HEADER    MEMBRANE PROTEIN                        23-MAR-22   7ZBC              
TITLE     DARK STATE CRYSTAL STRUCTURE OF BOVINE RHODOPSIN IN LIPIDIC CUBIC     
TITLE    2 PHASE (SACLA)                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RHODOPSIN;                                                 
COMPND   3 CHAIN: A, B                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: CATTLE;                                             
SOURCE   4 ORGANISM_TAXID: 9913                                                 
KEYWDS    GPCR, OPSIN, MEMBRANE PROTEIN                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.GRUHL,T.WEINERT,M.J.RODRIGUES,C.MILNE,G.ORTOLANI,K.NASS,E.NANGO,    
AUTHOR   2 S.SEN,P.JOHNSON,C.CIRELLI,A.FURRER,S.MOUS,P.SKOPINTSEV,D.JAMES,      
AUTHOR   3 F.DWORKOWSKI,P.BAATH,D.KEKILLI,D.OSEROV,R.TANAKA,H.GLOVER,           
AUTHOR   4 C.BACELLAR,S.BRUENLE,C.CASADEI,A.DIETHELM,D.GASHI,G.GOTTHARD,        
AUTHOR   5 R.GUIXA-GONZALEZ,Y.JOTI,V.KABANOVA,G.KNOPP,E.LESCA,P.MA,I.MARTIEL,   
AUTHOR   6 J.MUEHLE,S.OWADA,F.PAMULA,S.SARABI,O.TEJERO,C.J.TSAI,N.VARMA,A.WACH, 
AUTHOR   7 S.BOUTET,K.TONO,P.NOGLY,X.DEUPI,S.IWATA,R.NEUTZE,J.STANDFUSS,        
AUTHOR   8 G.F.X.SCHERTLER,V.PANNEELS                                           
REVDAT   3   12-APR-23 7ZBC    1       JRNL                                     
REVDAT   2   05-APR-23 7ZBC    1       JRNL                                     
REVDAT   1   29-MAR-23 7ZBC    0                                                
JRNL        AUTH   T.GRUHL,T.WEINERT,M.J.RODRIGUES,C.J.MILNE,G.ORTOLANI,K.NASS, 
JRNL        AUTH 2 E.NANGO,S.SEN,P.J.M.JOHNSON,C.CIRELLI,A.FURRER,S.MOUS,       
JRNL        AUTH 3 P.SKOPINTSEV,D.JAMES,F.DWORKOWSKI,P.BATH,D.KEKILLI,D.OZEROV, 
JRNL        AUTH 4 R.TANAKA,H.GLOVER,C.BACELLAR,S.BRUNLE,C.M.CASADEI,           
JRNL        AUTH 5 A.D.DIETHELM,D.GASHI,G.GOTTHARD,R.GUIXA-GONZALEZ,Y.JOTI,     
JRNL        AUTH 6 V.KABANOVA,G.KNOPP,E.LESCA,P.MA,I.MARTIEL,J.MUHLE,S.OWADA,   
JRNL        AUTH 7 F.PAMULA,D.SARABI,O.TEJERO,C.J.TSAI,N.VARMA,A.WACH,S.BOUTET, 
JRNL        AUTH 8 K.TONO,P.NOGLY,X.DEUPI,S.IWATA,R.NEUTZE,J.STANDFUSS,         
JRNL        AUTH 9 G.SCHERTLER,V.PANNEELS                                       
JRNL        TITL   ULTRAFAST STRUCTURAL CHANGES DIRECT THE FIRST MOLECULAR      
JRNL        TITL 2 EVENTS OF VISION.                                            
JRNL        REF    NATURE                        V. 615   939 2023              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   36949205                                                     
JRNL        DOI    10.1038/S41586-023-05863-6                                   
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.GRUHL,T.WEINERT,M.RODRIGUES,C.J.MILNE,G.ORTOLANI,K.NASS,   
REMARK   1  AUTH 2 E.NANGO,S.SEN,P.J.M.JOHNSON,C.CIRELLI,A.FURRER,S.MOUS,       
REMARK   1  AUTH 3 P.SKOPINTSEV,D.JAMES,F.DWORKOWSKI,P.BATH,D.KEKILLI,D.OZEROV, 
REMARK   1  AUTH 4 R.TANAKA,H.GLOVER,C.BACELLAR,S.BRUNLE,C.M.CASADEI,           
REMARK   1  AUTH 5 A.D.DIETHELM,D.GASHI,G.GOTTHARD,R.GUIXA-GONZALEZ,Y.JOTI,     
REMARK   1  AUTH 6 V.KABANOVA,G.KNOPP,E.LESCA,P.MA,I.MARTIEL,J.MUHLE,S.OWADA,   
REMARK   1  AUTH 7 F.PAMULA,D.SARABI,O.TEJERO,C.J.TSAI,N.VARMA,A.WACH,S.BOUTET, 
REMARK   1  AUTH 8 K.TONO,P.NOGLY,X.DEUPI,S.IWATA,R.NEUTZE,J.STANDFUSS,         
REMARK   1  AUTH 9 G.F.SCHERTLER,V.PANNEELS                                     
REMARK   1  TITL   ULTRAFAST STRUCTURAL CHANGES DIRECT THE FIRST MOLECULAR      
REMARK   1  TITL 2 EVENTS OF VISION                                             
REMARK   1  REF    BIORXIV                                    2022              
REMARK   1  REFN                   ISSN 2692-8205                               
REMARK   1  DOI    10.1101/2022.10.14.511948                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.19.2_4158                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.47                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 77918                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.450                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1127                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 10.4700 -  3.5600    0.98     9782   146  0.2047 0.2148        
REMARK   3     2  3.5600 -  2.8400    1.00     9704   142  0.1803 0.2049        
REMARK   3     3  2.8400 -  2.4900    1.00     9613   141  0.1690 0.2009        
REMARK   3     4  2.4900 -  2.2600    1.00     9589   139  0.1771 0.2086        
REMARK   3     5  2.2600 -  2.1000    1.00     9548   141  0.1848 0.2270        
REMARK   3     6  2.1000 -  1.9800    1.00     9510   140  0.2135 0.2694        
REMARK   3     7  1.9800 -  1.8800    1.00     9551   140  0.2552 0.3070        
REMARK   3     8  1.8800 -  1.8000    1.00     9494   138  0.3067 0.3330        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.197            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.188           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.71                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.46                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           5501                                  
REMARK   3   ANGLE     :  0.958           7457                                  
REMARK   3   CHIRALITY :  0.061            828                                  
REMARK   3   PLANARITY :  0.008            912                                  
REMARK   3   DIHEDRAL  : 12.902           2005                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.3841  28.2564  37.4549              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2169 T22:   0.1936                                     
REMARK   3      T33:   0.2162 T12:  -0.0195                                     
REMARK   3      T13:  -0.0124 T23:  -0.0090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6715 L22:   0.4224                                     
REMARK   3      L33:   0.3682 L12:  -0.2104                                     
REMARK   3      L13:  -0.3183 L23:   0.0650                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0085 S12:   0.0244 S13:   0.0058                       
REMARK   3      S21:   0.0017 S22:  -0.0070 S23:  -0.0085                       
REMARK   3      S31:   0.0132 S32:  -0.0225 S33:   0.0004                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7ZBC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-APR-22.                  
REMARK 100 THE DEPOSITION ID IS D_1292121333.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 294                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : FREE ELECTRON LASER                
REMARK 200  BEAMLINE                       : BL3                                
REMARK 200  X-RAY GENERATOR MODEL          : SACLA BEAMLINE BL3                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.24                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MPCCD                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL                           
REMARK 200  DATA SCALING SOFTWARE          : CRYSTFEL                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 78209                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.470                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 1342.                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.8700                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 963.9                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1U19                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 36 % PEG 600, 100 MM BICINE PH 9.0,      
REMARK 280  LIPIDIC CUBIC PHASE, TEMPERATURE 294K                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.40500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.25500            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.40500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       75.25500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   143                                                      
REMARK 465     SER A   144                                                      
REMARK 465     ASN A   145                                                      
REMARK 465     PHE A   146                                                      
REMARK 465     VAL A   230                                                      
REMARK 465     LYS A   231                                                      
REMARK 465     GLU A   232                                                      
REMARK 465     ALA A   233                                                      
REMARK 465     ALA A   234                                                      
REMARK 465     ALA A   235                                                      
REMARK 465     GLN A   236                                                      
REMARK 465     GLN A   237                                                      
REMARK 465     GLN A   238                                                      
REMARK 465     GLU A   239                                                      
REMARK 465     SER A   240                                                      
REMARK 465     ALA A   241                                                      
REMARK 465     THR A   242                                                      
REMARK 465     THR A   243                                                      
REMARK 465     GLN A   244                                                      
REMARK 465     CYS A   323                                                      
REMARK 465     GLY A   324                                                      
REMARK 465     LYS A   325                                                      
REMARK 465     ASN A   326                                                      
REMARK 465     PRO A   327                                                      
REMARK 465     LEU A   328                                                      
REMARK 465     GLY A   329                                                      
REMARK 465     ASP A   330                                                      
REMARK 465     ASP A   331                                                      
REMARK 465     GLU A   332                                                      
REMARK 465     ALA A   333                                                      
REMARK 465     SER A   334                                                      
REMARK 465     THR A   335                                                      
REMARK 465     THR A   336                                                      
REMARK 465     VAL A   337                                                      
REMARK 465     SER A   338                                                      
REMARK 465     LYS A   339                                                      
REMARK 465     THR A   340                                                      
REMARK 465     GLU A   341                                                      
REMARK 465     THR A   342                                                      
REMARK 465     SER A   343                                                      
REMARK 465     GLN A   344                                                      
REMARK 465     VAL A   345                                                      
REMARK 465     ALA A   346                                                      
REMARK 465     PRO A   347                                                      
REMARK 465     ALA A   348                                                      
REMARK 465     MET B   143                                                      
REMARK 465     SER B   144                                                      
REMARK 465     ASN B   145                                                      
REMARK 465     PHE B   146                                                      
REMARK 465     VAL B   230                                                      
REMARK 465     LYS B   231                                                      
REMARK 465     GLU B   232                                                      
REMARK 465     ALA B   233                                                      
REMARK 465     ALA B   234                                                      
REMARK 465     ALA B   235                                                      
REMARK 465     GLN B   236                                                      
REMARK 465     GLN B   237                                                      
REMARK 465     GLN B   238                                                      
REMARK 465     GLU B   239                                                      
REMARK 465     SER B   240                                                      
REMARK 465     ALA B   241                                                      
REMARK 465     THR B   242                                                      
REMARK 465     THR B   243                                                      
REMARK 465     CYS B   323                                                      
REMARK 465     GLY B   324                                                      
REMARK 465     LYS B   325                                                      
REMARK 465     ASN B   326                                                      
REMARK 465     PRO B   327                                                      
REMARK 465     LEU B   328                                                      
REMARK 465     GLY B   329                                                      
REMARK 465     ASP B   330                                                      
REMARK 465     ASP B   331                                                      
REMARK 465     GLU B   332                                                      
REMARK 465     ALA B   333                                                      
REMARK 465     SER B   334                                                      
REMARK 465     THR B   335                                                      
REMARK 465     THR B   336                                                      
REMARK 465     VAL B   337                                                      
REMARK 465     SER B   338                                                      
REMARK 465     LYS B   339                                                      
REMARK 465     THR B   340                                                      
REMARK 465     GLU B   341                                                      
REMARK 465     THR B   342                                                      
REMARK 465     SER B   343                                                      
REMARK 465     GLN B   344                                                      
REMARK 465     VAL B   345                                                      
REMARK 465     ALA B   346                                                      
REMARK 465     PRO B   347                                                      
REMARK 465     ALA B   348                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     MET A   1    CG   SD   CE                                        
REMARK 470     LYS A  66    CG   CD   CE   NZ                                   
REMARK 470     LYS A  67    CD   CE   NZ                                        
REMARK 470     ARG A 147    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 228    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 245    CE   NZ                                             
REMARK 470     MET B   1    CG   SD   CE                                        
REMARK 470     LYS B  67    CE   NZ                                             
REMARK 470     ARG B 147    CD   NE   CZ   NH1  NH2                             
REMARK 470     PHE B 228    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR B 229    OG1  CG2                                            
REMARK 470     GLN B 244    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 245    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   SG   CYS B   322     O2   PLM B   406              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A   8       30.65   -140.20                                   
REMARK 500    GLN A  28       37.37    -92.10                                   
REMARK 500    SER A 176     -166.15     61.11                                   
REMARK 500    HIS A 195       69.40     35.31                                   
REMARK 500    PHE A 212      -53.55   -136.28                                   
REMARK 500    PHE A 212      -51.70   -136.28                                   
REMARK 500    PHE A 228       47.45    -86.40                                   
REMARK 500    GLN B  28       35.31    -94.73                                   
REMARK 500    LYS B 141       59.25     39.01                                   
REMARK 500    LYS B 141       58.59     39.50                                   
REMARK 500    SER B 176     -165.52     60.62                                   
REMARK 500    HIS B 195       70.06     31.87                                   
REMARK 500    PHE B 212      -56.79   -140.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLC A  406                                                       
REMARK 610     OLC A  407                                                       
REMARK 610     OLC A  408                                                       
REMARK 610     OLC A  409                                                       
REMARK 610     OLC A  411                                                       
REMARK 610     OLC A  413                                                       
REMARK 610     OLC A  415                                                       
REMARK 610     OLC B  404                                                       
REMARK 610     OLC B  405                                                       
REMARK 610     PLM B  406                                                       
REMARK 610     OLC B  407                                                       
DBREF  7ZBC A    1   348  UNP    P02699   OPSD_BOVIN       1    348             
DBREF  7ZBC B    1   348  UNP    P02699   OPSD_BOVIN       1    348             
SEQRES   1 A  348  MET ASN GLY THR GLU GLY PRO ASN PHE TYR VAL PRO PHE          
SEQRES   2 A  348  SER ASN LYS THR GLY VAL VAL ARG SER PRO PHE GLU ALA          
SEQRES   3 A  348  PRO GLN TYR TYR LEU ALA GLU PRO TRP GLN PHE SER MET          
SEQRES   4 A  348  LEU ALA ALA TYR MET PHE LEU LEU ILE MET LEU GLY PHE          
SEQRES   5 A  348  PRO ILE ASN PHE LEU THR LEU TYR VAL THR VAL GLN HIS          
SEQRES   6 A  348  LYS LYS LEU ARG THR PRO LEU ASN TYR ILE LEU LEU ASN          
SEQRES   7 A  348  LEU ALA VAL ALA ASP LEU PHE MET VAL PHE GLY GLY PHE          
SEQRES   8 A  348  THR THR THR LEU TYR THR SER LEU HIS GLY TYR PHE VAL          
SEQRES   9 A  348  PHE GLY PRO THR GLY CYS ASN LEU GLU GLY PHE PHE ALA          
SEQRES  10 A  348  THR LEU GLY GLY GLU ILE ALA LEU TRP SER LEU VAL VAL          
SEQRES  11 A  348  LEU ALA ILE GLU ARG TYR VAL VAL VAL CYS LYS PRO MET          
SEQRES  12 A  348  SER ASN PHE ARG PHE GLY GLU ASN HIS ALA ILE MET GLY          
SEQRES  13 A  348  VAL ALA PHE THR TRP VAL MET ALA LEU ALA CYS ALA ALA          
SEQRES  14 A  348  PRO PRO LEU VAL GLY TRP SER ARG TYR ILE PRO GLU GLY          
SEQRES  15 A  348  MET GLN CYS SER CYS GLY ILE ASP TYR TYR THR PRO HIS          
SEQRES  16 A  348  GLU GLU THR ASN ASN GLU SER PHE VAL ILE TYR MET PHE          
SEQRES  17 A  348  VAL VAL HIS PHE ILE ILE PRO LEU ILE VAL ILE PHE PHE          
SEQRES  18 A  348  CYS TYR GLY GLN LEU VAL PHE THR VAL LYS GLU ALA ALA          
SEQRES  19 A  348  ALA GLN GLN GLN GLU SER ALA THR THR GLN LYS ALA GLU          
SEQRES  20 A  348  LYS GLU VAL THR ARG MET VAL ILE ILE MET VAL ILE ALA          
SEQRES  21 A  348  PHE LEU ILE CYS TRP LEU PRO TYR ALA GLY VAL ALA PHE          
SEQRES  22 A  348  TYR ILE PHE THR HIS GLN GLY SER ASP PHE GLY PRO ILE          
SEQRES  23 A  348  PHE MET THR ILE PRO ALA PHE PHE ALA LYS THR SER ALA          
SEQRES  24 A  348  VAL TYR ASN PRO VAL ILE TYR ILE MET MET ASN LYS GLN          
SEQRES  25 A  348  PHE ARG ASN CYS MET VAL THR THR LEU CYS CYS GLY LYS          
SEQRES  26 A  348  ASN PRO LEU GLY ASP ASP GLU ALA SER THR THR VAL SER          
SEQRES  27 A  348  LYS THR GLU THR SER GLN VAL ALA PRO ALA                      
SEQRES   1 B  348  MET ASN GLY THR GLU GLY PRO ASN PHE TYR VAL PRO PHE          
SEQRES   2 B  348  SER ASN LYS THR GLY VAL VAL ARG SER PRO PHE GLU ALA          
SEQRES   3 B  348  PRO GLN TYR TYR LEU ALA GLU PRO TRP GLN PHE SER MET          
SEQRES   4 B  348  LEU ALA ALA TYR MET PHE LEU LEU ILE MET LEU GLY PHE          
SEQRES   5 B  348  PRO ILE ASN PHE LEU THR LEU TYR VAL THR VAL GLN HIS          
SEQRES   6 B  348  LYS LYS LEU ARG THR PRO LEU ASN TYR ILE LEU LEU ASN          
SEQRES   7 B  348  LEU ALA VAL ALA ASP LEU PHE MET VAL PHE GLY GLY PHE          
SEQRES   8 B  348  THR THR THR LEU TYR THR SER LEU HIS GLY TYR PHE VAL          
SEQRES   9 B  348  PHE GLY PRO THR GLY CYS ASN LEU GLU GLY PHE PHE ALA          
SEQRES  10 B  348  THR LEU GLY GLY GLU ILE ALA LEU TRP SER LEU VAL VAL          
SEQRES  11 B  348  LEU ALA ILE GLU ARG TYR VAL VAL VAL CYS LYS PRO MET          
SEQRES  12 B  348  SER ASN PHE ARG PHE GLY GLU ASN HIS ALA ILE MET GLY          
SEQRES  13 B  348  VAL ALA PHE THR TRP VAL MET ALA LEU ALA CYS ALA ALA          
SEQRES  14 B  348  PRO PRO LEU VAL GLY TRP SER ARG TYR ILE PRO GLU GLY          
SEQRES  15 B  348  MET GLN CYS SER CYS GLY ILE ASP TYR TYR THR PRO HIS          
SEQRES  16 B  348  GLU GLU THR ASN ASN GLU SER PHE VAL ILE TYR MET PHE          
SEQRES  17 B  348  VAL VAL HIS PHE ILE ILE PRO LEU ILE VAL ILE PHE PHE          
SEQRES  18 B  348  CYS TYR GLY GLN LEU VAL PHE THR VAL LYS GLU ALA ALA          
SEQRES  19 B  348  ALA GLN GLN GLN GLU SER ALA THR THR GLN LYS ALA GLU          
SEQRES  20 B  348  LYS GLU VAL THR ARG MET VAL ILE ILE MET VAL ILE ALA          
SEQRES  21 B  348  PHE LEU ILE CYS TRP LEU PRO TYR ALA GLY VAL ALA PHE          
SEQRES  22 B  348  TYR ILE PHE THR HIS GLN GLY SER ASP PHE GLY PRO ILE          
SEQRES  23 B  348  PHE MET THR ILE PRO ALA PHE PHE ALA LYS THR SER ALA          
SEQRES  24 B  348  VAL TYR ASN PRO VAL ILE TYR ILE MET MET ASN LYS GLN          
SEQRES  25 B  348  PHE ARG ASN CYS MET VAL THR THR LEU CYS CYS GLY LYS          
SEQRES  26 B  348  ASN PRO LEU GLY ASP ASP GLU ALA SER THR THR VAL SER          
SEQRES  27 B  348  LYS THR GLU THR SER GLN VAL ALA PRO ALA                      
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    ACE  A 401       3                                                       
HET    RET  A 402      20                                                       
HET    NAG  A 403      14                                                       
HET    DAO  A 404      14                                                       
HET    OLC  A 405      25                                                       
HET    OLC  A 406      22                                                       
HET    OLC  A 407       7                                                       
HET    OLC  A 408      10                                                       
HET    OLC  A 409      12                                                       
HET    PLM  A 410      17                                                       
HET    OLC  A 411      10                                                       
HET    OLC  A 412      25                                                       
HET    OLC  A 413      10                                                       
HET    OLC  A 414      25                                                       
HET    OLC  A 415      13                                                       
HET    ACE  B 401       3                                                       
HET    RET  B 402      20                                                       
HET    NAG  B 403      14                                                       
HET    OLC  B 404      19                                                       
HET    OLC  B 405      18                                                       
HET    PLM  B 406       7                                                       
HET    OLC  B 407       7                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     RET RETINAL                                                          
HETNAM     DAO LAURIC ACID                                                      
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     PLM PALMITIC ACID                                                    
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   3  NAG    6(C8 H15 N O6)                                               
FORMUL   5  ACE    2(C2 H4 O)                                                   
FORMUL   6  RET    2(C20 H28 O)                                                 
FORMUL   8  DAO    C12 H24 O2                                                   
FORMUL   9  OLC    13(C21 H40 O4)                                               
FORMUL  14  PLM    2(C16 H32 O2)                                                
FORMUL  27  HOH   *168(H2 O)                                                    
HELIX    1 AA1 GLU A   33  HIS A   65  1                                  33    
HELIX    2 AA2 THR A   70  GLY A   90  1                                  21    
HELIX    3 AA3 GLY A   90  GLY A  101  1                                  12    
HELIX    4 AA4 PHE A  105  LYS A  141  1                                  37    
HELIX    5 AA5 GLY A  149  ALA A  169  1                                  21    
HELIX    6 AA6 PRO A  170  VAL A  173  5                                   4    
HELIX    7 AA7 HIS A  195  THR A  198  5                                   4    
HELIX    8 AA8 ASN A  199  HIS A  211  1                                  13    
HELIX    9 AA9 PHE A  212  PHE A  228  1                                  17    
HELIX   10 AB1 ALA A  246  HIS A  278  1                                  33    
HELIX   11 AB2 PRO A  285  ALA A  295  1                                  11    
HELIX   12 AB3 LYS A  296  ALA A  299  5                                   4    
HELIX   13 AB4 VAL A  300  ASN A  310  1                                  11    
HELIX   14 AB5 ASN A  310  CYS A  322  1                                  13    
HELIX   15 AB6 GLU B   33  HIS B   65  1                                  33    
HELIX   16 AB7 THR B   70  GLY B   90  1                                  21    
HELIX   17 AB8 GLY B   90  GLY B  101  1                                  12    
HELIX   18 AB9 PHE B  105  LYS B  141  1                                  37    
HELIX   19 AC1 GLY B  149  ALA B  169  1                                  21    
HELIX   20 AC2 PRO B  170  VAL B  173  5                                   4    
HELIX   21 AC3 HIS B  195  THR B  198  5                                   4    
HELIX   22 AC4 ASN B  199  HIS B  211  1                                  13    
HELIX   23 AC5 PHE B  212  PHE B  228  1                                  17    
HELIX   24 AC6 LYS B  245  HIS B  278  1                                  34    
HELIX   25 AC7 PRO B  285  ALA B  295  1                                  11    
HELIX   26 AC8 LYS B  296  ALA B  299  5                                   4    
HELIX   27 AC9 VAL B  300  ASN B  310  1                                  11    
HELIX   28 AD1 ASN B  310  CYS B  322  1                                  13    
SHEET    1 AA1 2 THR A   4  GLY A   6  0                                        
SHEET    2 AA1 2 PHE A   9  VAL A  11 -1  O  VAL A  11   N  THR A   4           
SHEET    1 AA2 2 TYR A 178  GLU A 181  0                                        
SHEET    2 AA2 2 SER A 186  ILE A 189 -1  O  SER A 186   N  GLU A 181           
SHEET    1 AA3 2 THR B   4  GLU B   5  0                                        
SHEET    2 AA3 2 TYR B  10  VAL B  11 -1  O  VAL B  11   N  THR B   4           
SHEET    1 AA4 2 TYR B 178  GLU B 181  0                                        
SHEET    2 AA4 2 SER B 186  ILE B 189 -1  O  GLY B 188   N  ILE B 179           
SSBOND   1 CYS A  110    CYS A  187                          1555   1555  2.05  
SSBOND   2 CYS B  110    CYS B  187                          1555   1555  2.03  
LINK         N   MET A   1                 C   ACE A 401     1555   1555  1.34  
LINK         ND2 ASN A   2                 C1  NAG A 403     1555   1555  1.46  
LINK         ND2 ASN A  15                 C1  NAG C   1     1555   1555  1.44  
LINK         NZ  LYS A 296                 C15 RET A 402     1555   1555  1.33  
LINK         SG  CYS A 322                 C1  PLM A 410     1555   1555  1.77  
LINK         N   MET B   1                 C   ACE B 401     1555   1555  1.33  
LINK         ND2 ASN B   2                 C1  NAG B 403     1555   1555  1.45  
LINK         ND2 ASN B  15                 C1  NAG D   1     1555   1555  1.43  
LINK         NZ  LYS B 296                 C15 RET B 402     1555   1555  1.34  
LINK         SG  CYS B 322                 C1  PLM B 406     1555   1555  1.77  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.45  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.45  
CRYST1   61.290   90.810  150.510  90.00  90.00  90.00 P 2 21 21     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016316  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011012  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006644        0.00000                         
ATOM      1  N   MET A   1      16.244  34.456   5.203  1.00 74.58           N  
ANISOU    1  N   MET A   1     9690   9448   9199    444    981    688       N  
ATOM      2  CA  MET A   1      15.816  33.367   6.087  1.00 66.48           C  
ANISOU    2  CA  MET A   1     8654   8432   8174    399    900    607       C  
ATOM      3  C   MET A   1      16.534  32.053   5.795  1.00 67.81           C  
ANISOU    3  C   MET A   1     8824   8614   8326    391    901    560       C  
ATOM      4  O   MET A   1      16.495  31.514   4.686  1.00 69.58           O  
ANISOU    4  O   MET A   1     9077   8892   8468    430    920    558       O  
ATOM      5  CB  MET A   1      14.303  33.160   5.992  1.00 72.96           C  
ANISOU    5  CB  MET A   1     9498   9316   8910    415    835    583       C  
ATOM      6  N   ASN A   2      17.191  31.547   6.823  1.00 58.15           N  
ANISOU    6  N   ASN A   2     7569   7343   7182    341    881    521       N  
ATOM      7  CA  ASN A   2      18.026  30.364   6.733  1.00 45.33           C  
ANISOU    7  CA  ASN A   2     5940   5718   5567    330    887    480       C  
ATOM      8  C   ASN A   2      17.272  29.077   7.056  1.00 41.60           C  
ANISOU    8  C   ASN A   2     5479   5279   5048    312    818    407       C  
ATOM      9  O   ASN A   2      17.864  27.991   7.008  1.00 42.57           O  
ANISOU    9  O   ASN A   2     5600   5400   5175    303    820    368       O  
ATOM     10  CB  ASN A   2      19.212  30.554   7.674  1.00 43.73           C  
ANISOU   10  CB  ASN A   2     5692   5446   5478    290    906    482       C  
ATOM     11  CG  ASN A   2      20.198  31.593   7.153  1.00 47.86           C  
ANISOU   11  CG  ASN A   2     6202   5933   6050    307    990    547       C  
ATOM     12  OD1 ASN A   2      21.021  31.267   6.309  1.00 45.40           O  
ANISOU   12  OD1 ASN A   2     5895   5628   5726    331   1045    562       O  
ATOM     13  ND2 ASN A   2      20.115  32.840   7.649  1.00 43.36           N  
ANISOU   13  ND2 ASN A   2     5613   5324   5538    295   1003    585       N  
ATOM     14  N   GLY A   3      15.986  29.184   7.371  1.00 33.79           N  
ANISOU   14  N   GLY A   3     4502   4319   4020    308    761    388       N  
ATOM     15  CA  GLY A   3      15.163  28.063   7.792  1.00 32.64           C  
ANISOU   15  CA  GLY A   3     4363   4199   3841    287    695    320       C  
ATOM     16  C   GLY A   3      13.950  27.950   6.890  1.00 32.34           C  
ANISOU   16  C   GLY A   3     4357   4234   3698    320    670    307       C  
ATOM     17  O   GLY A   3      13.894  28.602   5.846  1.00 33.79           O  
ANISOU   17  O   GLY A   3     4559   4452   3827    366    708    353       O  
ATOM     18  N   THR A   4      12.971  27.138   7.269  1.00 25.90           N  
ANISOU   18  N   THR A   4     3545   3444   2851    300    609    248       N  
ATOM     19  CA  THR A   4      11.821  26.855   6.414  1.00 25.67           C  
ANISOU   19  CA  THR A   4     3541   3491   2722    328    580    222       C  
ATOM     20  C   THR A   4      10.547  27.109   7.208  1.00 32.35           C  
ANISOU   20  C   THR A   4     4377   4345   3568    308    517    204       C  
ATOM     21  O   THR A   4      10.223  26.352   8.124  1.00 28.61           O  
ANISOU   21  O   THR A   4     3891   3850   3129    266    474    153       O  
ATOM     22  CB  THR A   4      11.896  25.413   5.909  1.00 27.26           C  
ANISOU   22  CB  THR A   4     3755   3720   2883    324    572    153       C  
ATOM     23  OG1 THR A   4      13.124  25.243   5.179  1.00 25.21           O  
ANISOU   23  OG1 THR A   4     3504   3450   2626    346    635    173       O  
ATOM     24  CG2 THR A   4      10.721  25.090   4.980  1.00 27.94           C  
ANISOU   24  CG2 THR A   4     3863   3891   2863    352    540    116       C  
ATOM     25  N   GLU A   5       9.817  28.168   6.870  1.00 26.48           N  
ANISOU   25  N   GLU A   5     3639   3633   2788    339    514    249       N  
ATOM     26  CA  GLU A   5       8.586  28.459   7.586  1.00 29.80           C  
ANISOU   26  CA  GLU A   5     4051   4065   3208    323    457    235       C  
ATOM     27  C   GLU A   5       7.418  27.754   6.907  1.00 34.04           C  
ANISOU   27  C   GLU A   5     4600   4681   3654    338    412    183       C  
ATOM     28  O   GLU A   5       7.312  27.742   5.682  1.00 33.40           O  
ANISOU   28  O   GLU A   5     4538   4663   3491    383    429    190       O  
ATOM     29  CB  GLU A   5       8.328  29.971   7.645  1.00 28.90           C  
ANISOU   29  CB  GLU A   5     3934   3941   3107    348    475    308       C  
ATOM     30  CG  GLU A   5       7.145  30.346   8.547  1.00 34.32           C  
ANISOU   30  CG  GLU A   5     4606   4627   3808    328    421    297       C  
ATOM     31  CD  GLU A   5       6.880  31.847   8.602  1.00 36.05           C  
ANISOU   31  CD  GLU A   5     4823   4832   4043    355    443    369       C  
ATOM     32  OE1 GLU A   5       7.685  32.609   8.055  1.00 42.22           O  
ANISOU   32  OE1 GLU A   5     5612   5594   4837    383    504    429       O  
ATOM     33  OE2 GLU A   5       5.862  32.259   9.204  1.00 38.85           O  
ANISOU   33  OE2 GLU A   5     5169   5191   4402    348    404    366       O  
ATOM     34  N   GLY A   6       6.555  27.145   7.708  1.00 30.99           N  
ANISOU   34  N   GLY A   6     4200   4294   3281    301    356    127       N  
ATOM     35  CA  GLY A   6       5.311  26.625   7.201  1.00 29.57           C  
ANISOU   35  CA  GLY A   6     4024   4186   3024    310    309     77       C  
ATOM     36  C   GLY A   6       4.163  27.334   7.882  1.00 31.93           C  
ANISOU   36  C   GLY A   6     4307   4492   3332    304    266     90       C  
ATOM     37  O   GLY A   6       4.370  28.282   8.653  1.00 30.78           O  
ANISOU   37  O   GLY A   6     4152   4296   3246    297    278    140       O  
ATOM     38  N   PRO A   7       2.930  26.871   7.637  1.00 30.65           N  
ANISOU   38  N   PRO A   7     4140   4392   3114    305    216     39       N  
ATOM     39  CA  PRO A   7       1.767  27.536   8.259  1.00 33.15           C  
ANISOU   39  CA  PRO A   7     4439   4719   3437    302    175     51       C  
ATOM     40  C   PRO A   7       1.828  27.547   9.771  1.00 32.85           C  
ANISOU   40  C   PRO A   7     4385   4604   3493    250    162     46       C  
ATOM     41  O   PRO A   7       1.384  28.513  10.407  1.00 29.67           O  
ANISOU   41  O   PRO A   7     3972   4181   3119    253    154     86       O  
ATOM     42  CB  PRO A   7       0.571  26.706   7.760  1.00 31.15           C  
ANISOU   42  CB  PRO A   7     4178   4543   3116    301    124    -22       C  
ATOM     43  CG  PRO A   7       1.076  25.986   6.532  1.00 36.65           C  
ANISOU   43  CG  PRO A   7     4894   5288   3746    325    144    -52       C  
ATOM     44  CD  PRO A   7       2.539  25.768   6.731  1.00 36.69           C  
ANISOU   44  CD  PRO A   7     4912   5222   3806    311    196    -32       C  
ATOM     45  N   ASN A   8       2.359  26.484  10.373  1.00 28.20           N  
ANISOU   45  N   ASN A   8     3793   3970   2951    207    161     -2       N  
ATOM     46  CA  ASN A   8       2.336  26.372  11.822  1.00 25.45           C  
ANISOU   46  CA  ASN A   8     3430   3558   2683    161    144    -11       C  
ATOM     47  C   ASN A   8       3.653  25.791  12.338  1.00 26.44           C  
ANISOU   47  C   ASN A   8     3557   3618   2870    134    175    -15       C  
ATOM     48  O   ASN A   8       3.673  25.088  13.353  1.00 27.26           O  
ANISOU   48  O   ASN A   8     3652   3681   3025     95    159    -48       O  
ATOM     49  CB  ASN A   8       1.140  25.521  12.270  1.00 28.96           C  
ANISOU   49  CB  ASN A   8     3861   4022   3119    130     94    -77       C  
ATOM     50  CG  ASN A   8       1.052  24.206  11.506  1.00 34.24           C  
ANISOU   50  CG  ASN A   8     4536   4727   3747    124     88   -146       C  
ATOM     51  OD1 ASN A   8       1.894  23.920  10.662  1.00 31.96           O  
ANISOU   51  OD1 ASN A   8     4264   4448   3432    142    120   -145       O  
ATOM     52  ND2 ASN A   8       0.052  23.392  11.821  1.00 35.72           N  
ANISOU   52  ND2 ASN A   8     4710   4930   3932     94     50   -209       N  
ATOM     53  N   PHE A   9       4.754  26.052  11.639  1.00 26.49           N  
ANISOU   53  N   PHE A   9     3575   3618   2872    159    221     20       N  
ATOM     54  CA  PHE A   9       6.044  25.540  12.075  1.00 24.43           C  
ANISOU   54  CA  PHE A   9     3313   3300   2670    138    252     19       C  
ATOM     55  C   PHE A   9       7.143  26.403  11.467  1.00 25.09           C  
ANISOU   55  C   PHE A   9     3402   3371   2761    168    306     80       C  
ATOM     56  O   PHE A   9       6.909  27.218  10.569  1.00 23.25           O  
ANISOU   56  O   PHE A   9     3179   3176   2477    208    323    119       O  
ATOM     57  CB  PHE A   9       6.217  24.062  11.693  1.00 23.29           C  
ANISOU   57  CB  PHE A   9     3177   3166   2507    125    251    -45       C  
ATOM     58  CG  PHE A   9       6.156  23.796  10.209  1.00 22.82           C  
ANISOU   58  CG  PHE A   9     3136   3168   2366    161    268    -59       C  
ATOM     59  CD1 PHE A   9       7.291  23.923   9.418  1.00 26.96           C  
ANISOU   59  CD1 PHE A   9     3673   3690   2882    188    319    -29       C  
ATOM     60  CD2 PHE A   9       4.981  23.385   9.612  1.00 28.89           C  
ANISOU   60  CD2 PHE A   9     3909   4001   3068    168    232   -106       C  
ATOM     61  CE1 PHE A   9       7.251  23.664   8.065  1.00 32.40           C  
ANISOU   61  CE1 PHE A   9     4381   4439   3491    223    336    -43       C  
ATOM     62  CE2 PHE A   9       4.931  23.124   8.240  1.00 30.35           C  
ANISOU   62  CE2 PHE A   9     4110   4250   3171    203    245   -125       C  
ATOM     63  CZ  PHE A   9       6.063  23.267   7.472  1.00 34.56           C  
ANISOU   63  CZ  PHE A   9     4660   4781   3692    232    297    -92       C  
ATOM     64  N   TYR A  10       8.348  26.228  12.002  1.00 24.50           N  
ANISOU   64  N   TYR A  10     3318   3240   2750    150    334     90       N  
ATOM     65  CA  TYR A  10       9.532  26.917  11.507  1.00 24.10           C  
ANISOU   65  CA  TYR A  10     3267   3168   2720    172    390    142       C  
ATOM     66  C   TYR A  10      10.668  25.929  11.722  1.00 25.64           C  
ANISOU   66  C   TYR A  10     3457   3329   2957    153    410    117       C  
ATOM     67  O   TYR A  10      11.134  25.764  12.853  1.00 23.43           O  
ANISOU   67  O   TYR A  10     3157   3001   2746    122    400    111       O  
ATOM     68  CB  TYR A  10       9.821  28.221  12.240  1.00 22.57           C  
ANISOU   68  CB  TYR A  10     3057   2932   2588    165    402    194       C  
ATOM     69  CG  TYR A  10      11.044  28.888  11.645  1.00 22.59           C  
ANISOU   69  CG  TYR A  10     3056   2911   2614    186    466    245       C  
ATOM     70  CD1 TYR A  10      10.916  29.704  10.532  1.00 30.03           C  
ANISOU   70  CD1 TYR A  10     4016   3886   3509    231    502    293       C  
ATOM     71  CD2 TYR A  10      12.341  28.634  12.142  1.00 24.23           C  
ANISOU   71  CD2 TYR A  10     3245   3069   2892    165    492    246       C  
ATOM     72  CE1 TYR A  10      12.023  30.281   9.929  1.00 29.86           C  
ANISOU   72  CE1 TYR A  10     3993   3842   3509    252    567    342       C  
ATOM     73  CE2 TYR A  10      13.470  29.232  11.537  1.00 26.07           C  
ANISOU   73  CE2 TYR A  10     3473   3282   3150    184    555    292       C  
ATOM     74  CZ  TYR A  10      13.285  30.056  10.430  1.00 28.41           C  
ANISOU   74  CZ  TYR A  10     3788   3606   3399    226    593    340       C  
ATOM     75  OH  TYR A  10      14.345  30.670   9.798  1.00 31.90           O  
ANISOU   75  OH  TYR A  10     4227   4028   3867    247    661    389       O  
ATOM     76  N   VAL A  11      11.113  25.295  10.647  1.00 23.40           N  
ANISOU   76  N   VAL A  11     3190   3072   2630    176    441    104       N  
ATOM     77  CA  VAL A  11      12.155  24.283  10.771  1.00 26.03           C  
ANISOU   77  CA  VAL A  11     3518   3373   2998    162    463     79       C  
ATOM     78  C   VAL A  11      13.504  24.971  10.621  1.00 23.62           C  
ANISOU   78  C   VAL A  11     3200   3034   2741    174    518    132       C  
ATOM     79  O   VAL A  11      13.718  25.664   9.623  1.00 24.53           O  
ANISOU   79  O   VAL A  11     3327   3172   2819    209    557    172       O  
ATOM     80  CB  VAL A  11      11.955  23.177   9.725  1.00 27.44           C  
ANISOU   80  CB  VAL A  11     3720   3594   3111    178    470     31       C  
ATOM     81  CG1 VAL A  11      13.099  22.206   9.777  1.00 29.48           C  
ANISOU   81  CG1 VAL A  11     3975   3818   3409    170    501     12       C  
ATOM     82  CG2 VAL A  11      10.593  22.455   9.996  1.00 22.69           C  
ANISOU   82  CG2 VAL A  11     3124   3022   2476    158    413    -29       C  
ATOM     83  N   PRO A  12      14.456  24.804  11.572  1.00 23.91           N  
ANISOU   83  N   PRO A  12     3210   3016   2857    149    525    135       N  
ATOM     84  CA  PRO A  12      15.772  25.469  11.439  1.00 23.83           C  
ANISOU   84  CA  PRO A  12     3182   2975   2899    157    578    181       C  
ATOM     85  C   PRO A  12      16.694  24.720  10.482  1.00 25.08           C  
ANISOU   85  C   PRO A  12     3350   3140   3040    179    626    175       C  
ATOM     86  O   PRO A  12      17.760  24.202  10.854  1.00 27.71           O  
ANISOU   86  O   PRO A  12     3661   3438   3428    168    646    170       O  
ATOM     87  CB  PRO A  12      16.285  25.473  12.887  1.00 27.88           C  
ANISOU   87  CB  PRO A  12     3660   3438   3497    121    555    176       C  
ATOM     88  CG  PRO A  12      15.671  24.254  13.500  1.00 29.26           C  
ANISOU   88  CG  PRO A  12     3841   3617   3661    102    509    122       C  
ATOM     89  CD  PRO A  12      14.332  24.051  12.840  1.00 21.84           C  
ANISOU   89  CD  PRO A  12     2932   2725   2642    113    483     98       C  
ATOM     90  N   PHE A  13      16.267  24.641   9.224  1.00 26.67           N  
ANISOU   90  N   PHE A  13     3582   3390   3161    213    645    175       N  
ATOM     91  CA  PHE A  13      16.948  23.850   8.212  1.00 26.14           C  
ANISOU   91  CA  PHE A  13     3530   3339   3062    236    688    161       C  
ATOM     92  C   PHE A  13      16.483  24.373   6.866  1.00 25.70           C  
ANISOU   92  C   PHE A  13     3506   3340   2919    280    714    184       C  
ATOM     93  O   PHE A  13      15.279  24.541   6.656  1.00 29.36           O  
ANISOU   93  O   PHE A  13     3986   3848   3322    288    675    171       O  
ATOM     94  CB  PHE A  13      16.606  22.358   8.376  1.00 26.36           C  
ANISOU   94  CB  PHE A  13     3569   3374   3073    220    659     90       C  
ATOM     95  CG  PHE A  13      17.520  21.426   7.608  1.00 25.86           C  
ANISOU   95  CG  PHE A  13     3515   3309   3000    237    706     71       C  
ATOM     96  CD1 PHE A  13      18.651  20.905   8.214  1.00 26.59           C  
ANISOU   96  CD1 PHE A  13     3583   3352   3167    223    727     71       C  
ATOM     97  CD2 PHE A  13      17.251  21.070   6.292  1.00 29.84           C  
ANISOU   97  CD2 PHE A  13     4052   3866   3420    269    728     51       C  
ATOM     98  CE1 PHE A  13      19.499  20.026   7.514  1.00 31.12           C  
ANISOU   98  CE1 PHE A  13     4166   3923   3736    241    774     53       C  
ATOM     99  CE2 PHE A  13      18.101  20.215   5.591  1.00 33.44           C  
ANISOU   99  CE2 PHE A  13     4518   4320   3868    286    774     30       C  
ATOM    100  CZ  PHE A  13      19.224  19.697   6.205  1.00 36.96           C  
ANISOU  100  CZ  PHE A  13     4940   4711   4393    271    798     32       C  
ATOM    101  N   SER A  14      17.423  24.645   5.972  1.00 25.87           N  
ANISOU  101  N   SER A  14     3533   3364   2933    311    779    221       N  
ATOM    102  CA  SER A  14      17.064  25.226   4.685  1.00 26.88           C  
ANISOU  102  CA  SER A  14     3690   3548   2976    360    809    254       C  
ATOM    103  C   SER A  14      16.394  24.195   3.787  1.00 27.75           C  
ANISOU  103  C   SER A  14     3832   3721   2990    379    791    195       C  
ATOM    104  O   SER A  14      16.804  23.032   3.741  1.00 30.98           O  
ANISOU  104  O   SER A  14     4244   4122   3404    367    795    144       O  
ATOM    105  CB  SER A  14      18.314  25.768   3.984  1.00 26.48           C  
ANISOU  105  CB  SER A  14     3636   3478   2946    388    891    311       C  
ATOM    106  OG  SER A  14      17.985  26.225   2.681  1.00 34.57           O  
ANISOU  106  OG  SER A  14     4693   4561   3880    441    924    343       O  
ATOM    107  N   ASN A  15      15.385  24.634   3.031  1.00 29.25           N  
ANISOU  107  N   ASN A  15     4045   3977   3091    412    774    202       N  
ATOM    108  CA  ASN A  15      14.748  23.752   2.063  1.00 28.22           C  
ANISOU  108  CA  ASN A  15     3943   3916   2861    434    758    144       C  
ATOM    109  C   ASN A  15      15.292  23.940   0.647  1.00 34.95           C  
ANISOU  109  C   ASN A  15     4822   4816   3642    490    820    175       C  
ATOM    110  O   ASN A  15      14.615  23.602  -0.334  1.00 30.56           O  
ANISOU  110  O   ASN A  15     4292   4336   2983    523    808    143       O  
ATOM    111  CB  ASN A  15      13.228  23.931   2.090  1.00 26.72           C  
ANISOU  111  CB  ASN A  15     3759   3783   2610    436    692    120       C  
ATOM    112  CG  ASN A  15      12.521  22.732   1.506  1.00 30.01           C  
ANISOU  112  CG  ASN A  15     4193   4258   2953    435    658     32       C  
ATOM    113  OD1 ASN A  15      13.073  21.635   1.524  1.00 29.15           O  
ANISOU  113  OD1 ASN A  15     4086   4125   2865    415    671    -19       O  
ATOM    114  ND2 ASN A  15      11.312  22.927   0.980  1.00 27.40           N  
ANISOU  114  ND2 ASN A  15     3872   4001   2536    457    617     14       N  
ATOM    115  N   LYS A  16      16.524  24.429   0.503  1.00 30.28           N  
ANISOU  115  N   LYS A  16     4223   4181   3100    503    889    234       N  
ATOM    116  CA  LYS A  16      17.049  24.605  -0.849  1.00 29.76           C  
ANISOU  116  CA  LYS A  16     4185   4159   2964    560    954    266       C  
ATOM    117  C   LYS A  16      17.129  23.282  -1.601  1.00 38.12           C  
ANISOU  117  C   LYS A  16     5265   5257   3960    569    957    192       C  
ATOM    118  O   LYS A  16      16.902  23.250  -2.816  1.00 37.01           O  
ANISOU  118  O   LYS A  16     5156   5190   3717    618    978    190       O  
ATOM    119  CB  LYS A  16      18.426  25.277  -0.798  1.00 39.04           C  
ANISOU  119  CB  LYS A  16     5343   5272   4218    565   1032    337       C  
ATOM    120  CG  LYS A  16      19.413  24.631   0.148  1.00 52.80           C  
ANISOU  120  CG  LYS A  16     7054   6940   6069    517   1038    312       C  
ATOM    121  CD  LYS A  16      20.631  25.525   0.355  1.00 61.02           C  
ANISOU  121  CD  LYS A  16     8069   7920   7198    518   1105    385       C  
ATOM    122  CE  LYS A  16      21.693  24.824   1.187  1.00 65.59           C  
ANISOU  122  CE  LYS A  16     8612   8432   7875    477   1113    359       C  
ATOM    123  NZ  LYS A  16      21.186  24.453   2.538  1.00 68.51           N  
ANISOU  123  NZ  LYS A  16     8959   8771   8301    425   1039    315       N  
ATOM    124  N   THR A  17      17.403  22.183  -0.902  1.00 32.05           N  
ANISOU  124  N   THR A  17     4483   4446   3249    524    935    128       N  
ATOM    125  CA  THR A  17      17.448  20.865  -1.526  1.00 36.72           C  
ANISOU  125  CA  THR A  17     5094   5066   3791    527    938     50       C  
ATOM    126  C   THR A  17      16.096  20.154  -1.538  1.00 32.78           C  
ANISOU  126  C   THR A  17     4605   4619   3230    511    866    -32       C  
ATOM    127  O   THR A  17      16.029  19.010  -1.995  1.00 33.62           O  
ANISOU  127  O   THR A  17     4726   4747   3302    507    864   -108       O  
ATOM    128  CB  THR A  17      18.475  19.969  -0.822  1.00 34.43           C  
ANISOU  128  CB  THR A  17     4783   4700   3597    491    960     23       C  
ATOM    129  OG1 THR A  17      18.078  19.769   0.548  1.00 34.46           O  
ANISOU  129  OG1 THR A  17     4760   4654   3678    438    903      2       O  
ATOM    130  CG2 THR A  17      19.865  20.581  -0.885  1.00 44.36           C  
ANISOU  130  CG2 THR A  17     6026   5912   4916    506   1034     96       C  
ATOM    131  N   GLY A  18      15.038  20.768  -1.008  1.00 28.34           N  
ANISOU  131  N   GLY A  18     4033   4073   2662    498    809    -22       N  
ATOM    132  CA  GLY A  18      13.704  20.221  -1.169  1.00 31.39           C  
ANISOU  132  CA  GLY A  18     4427   4519   2980    489    743    -95       C  
ATOM    133  C   GLY A  18      13.354  19.084  -0.234  1.00 36.45           C  
ANISOU  133  C   GLY A  18     5052   5117   3680    431    700   -174       C  
ATOM    134  O   GLY A  18      12.305  18.457  -0.417  1.00 30.94           O  
ANISOU  134  O   GLY A  18     4358   4465   2931    419    651   -247       O  
ATOM    135  N   VAL A  19      14.189  18.803   0.774  1.00 27.39           N  
ANISOU  135  N   VAL A  19     3885   3884   2639    396    716   -161       N  
ATOM    136  CA  VAL A  19      13.967  17.629   1.627  1.00 28.65           C  
ANISOU  136  CA  VAL A  19     4032   3998   2854    346    685   -232       C  
ATOM    137  C   VAL A  19      13.169  17.925   2.890  1.00 30.57           C  
ANISOU  137  C   VAL A  19     4252   4211   3151    306    627   -227       C  
ATOM    138  O   VAL A  19      12.797  16.980   3.610  1.00 30.65           O  
ANISOU  138  O   VAL A  19     4254   4190   3203    266    598   -285       O  
ATOM    139  CB  VAL A  19      15.307  16.976   2.034  1.00 34.54           C  
ANISOU  139  CB  VAL A  19     4769   4670   3682    333    734   -226       C  
ATOM    140  CG1 VAL A  19      16.102  16.524   0.794  1.00 31.78           C  
ANISOU  140  CG1 VAL A  19     4444   4348   3283    371    795   -240       C  
ATOM    141  CG2 VAL A  19      16.126  17.922   2.900  1.00 31.46           C  
ANISOU  141  CG2 VAL A  19     4354   4224   3376    327    751   -144       C  
ATOM    142  N   VAL A  20      12.868  19.192   3.178  1.00 27.13           N  
ANISOU  142  N   VAL A  20     3807   3784   2718    316    612   -162       N  
ATOM    143  CA  VAL A  20      12.189  19.526   4.428  1.00 25.39           C  
ANISOU  143  CA  VAL A  20     3565   3531   2553    280    562   -154       C  
ATOM    144  C   VAL A  20      10.739  19.079   4.375  1.00 29.95           C  
ANISOU  144  C   VAL A  20     4145   4157   3079    265    503   -219       C  
ATOM    145  O   VAL A  20      10.031  19.317   3.390  1.00 30.66           O  
ANISOU  145  O   VAL A  20     4248   4323   3078    296    490   -232       O  
ATOM    146  CB  VAL A  20      12.273  21.029   4.727  1.00 25.18           C  
ANISOU  146  CB  VAL A  20     3526   3496   2544    295    567    -69       C  
ATOM    147  CG1 VAL A  20      11.512  21.393   6.025  1.00 30.03           C  
ANISOU  147  CG1 VAL A  20     4118   4079   3211    258    514    -66       C  
ATOM    148  CG2 VAL A  20      13.726  21.456   4.782  1.00 30.91           C  
ANISOU  148  CG2 VAL A  20     4245   4172   3328    305    628    -11       C  
ATOM    149  N  AARG A  21      10.286  18.425   5.439  0.52 30.72           N  
ANISOU  149  N  AARG A  21     4226   4213   3233    220    467   -259       N  
ATOM    150  N  BARG A  21      10.286  18.450   5.457  0.48 30.70           N  
ANISOU  150  N  BARG A  21     4224   4210   3232    220    467   -258       N  
ATOM    151  CA AARG A  21       8.891  18.039   5.556  0.52 28.76           C  
ANISOU  151  CA AARG A  21     3975   4002   2952    200    412   -318       C  
ATOM    152  CA BARG A  21       8.915  17.991   5.593  0.48 28.79           C  
ANISOU  152  CA BARG A  21     3978   4002   2959    198    412   -320       C  
ATOM    153  C  AARG A  21       8.350  18.537   6.886  0.52 29.79           C  
ANISOU  153  C  AARG A  21     4083   4093   3144    168    373   -293       C  
ATOM    154  C  BARG A  21       8.352  18.525   6.902  0.48 29.78           C  
ANISOU  154  C  BARG A  21     4082   4091   3144    168    373   -293       C  
ATOM    155  O  AARG A  21       9.103  18.754   7.842  0.52 28.36           O  
ANISOU  155  O  AARG A  21     3890   3847   3040    152    388   -252       O  
ATOM    156  O  BARG A  21       9.094  18.754   7.863  0.48 28.36           O  
ANISOU  156  O  BARG A  21     3889   3846   3040    152    387   -252       O  
ATOM    157  CB AARG A  21       8.711  16.518   5.413  0.52 30.93           C  
ANISOU  157  CB AARG A  21     4254   4268   3228    173    410   -411       C  
ATOM    158  CB BARG A  21       8.854  16.457   5.539  0.48 30.59           C  
ANISOU  158  CB BARG A  21     4211   4214   3199    170    414   -408       C  
ATOM    159  CG AARG A  21       8.887  16.044   3.955  0.52 34.31           C  
ANISOU  159  CG AARG A  21     4706   4757   3574    205    436   -453       C  
ATOM    160  CG BARG A  21       9.545  15.890   4.285  0.48 34.25           C  
ANISOU  160  CG BARG A  21     4697   4707   3610    199    459   -437       C  
ATOM    161  CD AARG A  21       8.286  14.667   3.694  0.52 42.11           C  
ANISOU  161  CD AARG A  21     5697   5756   4548    177    421   -559       C  
ATOM    162  CD BARG A  21       9.482  14.374   4.210  0.48 40.71           C  
ANISOU  162  CD BARG A  21     5521   5505   4444    171    465   -528       C  
ATOM    163  NE AARG A  21       9.154  13.580   4.134  0.52 42.84           N  
ANISOU  163  NE AARG A  21     5792   5773   4713    154    459   -586       N  
ATOM    164  NE BARG A  21       8.129  13.895   3.955  0.48 44.42           N  
ANISOU  164  NE BARG A  21     5987   6024   4867    152    418   -606       N  
ATOM    165  CZ AARG A  21       8.907  12.293   3.933  0.52 44.95           C  
ANISOU  165  CZ AARG A  21     6065   6030   4986    129    464   -674       C  
ATOM    166  CZ BARG A  21       7.794  12.615   3.866  0.48 45.44           C  
ANISOU  166  CZ BARG A  21     6117   6140   5006    123    417   -696       C  
ATOM    167  NH1AARG A  21       7.819  11.888   3.294  0.52 47.73           N  
ANISOU  167  NH1AARG A  21     6417   6443   5275    122    430   -752       N  
ATOM    168  NH1BARG A  21       8.693  11.654   4.004  0.48 46.69           N  
ANISOU  168  NH1BARG A  21     6285   6238   5219    112    462   -718       N  
ATOM    169  NH2AARG A  21       9.773  11.388   4.382  0.52 45.45           N  
ANISOU  169  NH2AARG A  21     6130   6018   5119    113    504   -686       N  
ATOM    170  NH2BARG A  21       6.525  12.292   3.640  0.48 50.20           N  
ANISOU  170  NH2BARG A  21     6712   6793   5570    104    371   -766       N  
ATOM    171  N   SER A  22       7.045  18.755   6.925  1.00 27.07           N  
ANISOU  171  N   SER A  22     3731   3792   2761    162    324   -316       N  
ATOM    172  CA  SER A  22       6.428  19.314   8.122  1.00 27.28           C  
ANISOU  172  CA  SER A  22     3738   3789   2838    137    288   -291       C  
ATOM    173  C   SER A  22       6.639  18.377   9.309  1.00 26.32           C  
ANISOU  173  C   SER A  22     3606   3596   2800     91    284   -321       C  
ATOM    174  O   SER A  22       6.499  17.157   9.166  1.00 26.19           O  
ANISOU  174  O   SER A  22     3593   3573   2785     72    286   -388       O  
ATOM    175  CB  SER A  22       4.926  19.531   7.901  1.00 27.44           C  
ANISOU  175  CB  SER A  22     3750   3873   2803    138    236   -322       C  
ATOM    176  OG  SER A  22       4.269  19.749   9.122  1.00 25.62           O  
ANISOU  176  OG  SER A  22     3500   3607   2626    106    202   -316       O  
ATOM    177  N   PRO A  23       6.963  18.912  10.494  1.00 23.47           N  
ANISOU  177  N   PRO A  23     3230   3181   2507     75    280   -274       N  
ATOM    178  CA  PRO A  23       7.063  18.071  11.695  1.00 27.56           C  
ANISOU  178  CA  PRO A  23     3738   3637   3098     37    273   -297       C  
ATOM    179  C   PRO A  23       5.726  17.547  12.178  1.00 27.90           C  
ANISOU  179  C   PRO A  23     3773   3690   3139      7    231   -349       C  
ATOM    180  O   PRO A  23       5.695  16.815  13.167  1.00 25.78           O  
ANISOU  180  O   PRO A  23     3496   3371   2927    -23    227   -368       O  
ATOM    181  CB  PRO A  23       7.679  19.024  12.731  1.00 26.55           C  
ANISOU  181  CB  PRO A  23     3595   3465   3027     35    276   -229       C  
ATOM    182  CG  PRO A  23       7.173  20.366  12.337  1.00 25.83           C  
ANISOU  182  CG  PRO A  23     3503   3416   2896     58    262   -187       C  
ATOM    183  CD  PRO A  23       7.187  20.337  10.803  1.00 22.43           C  
ANISOU  183  CD  PRO A  23     3091   3044   2387     92    282   -199       C  
ATOM    184  N   PHE A  24       4.617  17.915  11.542  1.00 27.01           N  
ANISOU  184  N   PHE A  24     3659   3640   2965     16    200   -370       N  
ATOM    185  CA  PHE A  24       3.348  17.258  11.823  1.00 24.50           C  
ANISOU  185  CA  PHE A  24     3329   3336   2643    -13    163   -431       C  
ATOM    186  C   PHE A  24       3.001  16.199  10.802  1.00 30.34           C  
ANISOU  186  C   PHE A  24     4077   4114   3339    -17    166   -511       C  
ATOM    187  O   PHE A  24       1.935  15.583  10.914  1.00 29.09           O  
ANISOU  187  O   PHE A  24     3907   3970   3178    -44    138   -572       O  
ATOM    188  CB  PHE A  24       2.221  18.284  11.889  1.00 25.24           C  
ANISOU  188  CB  PHE A  24     3410   3477   2703     -5    122   -411       C  
ATOM    189  CG  PHE A  24       2.473  19.358  12.887  1.00 24.81           C  
ANISOU  189  CG  PHE A  24     3348   3386   2693     -3    119   -340       C  
ATOM    190  CD1 PHE A  24       2.543  19.055  14.238  1.00 27.43           C  
ANISOU  190  CD1 PHE A  24     3671   3656   3096    -35    114   -335       C  
ATOM    191  CD2 PHE A  24       2.641  20.675  12.482  1.00 29.74           C  
ANISOU  191  CD2 PHE A  24     3975   4039   3287     32    123   -278       C  
ATOM    192  CE1 PHE A  24       2.776  20.052  15.194  1.00 28.37           C  
ANISOU  192  CE1 PHE A  24     3782   3744   3254    -34    110   -275       C  
ATOM    193  CE2 PHE A  24       2.880  21.675  13.432  1.00 31.89           C  
ANISOU  193  CE2 PHE A  24     4239   4273   3605     31    122   -218       C  
ATOM    194  CZ  PHE A  24       2.939  21.366  14.779  1.00 27.95           C  
ANISOU  194  CZ  PHE A  24     3729   3716   3174     -3    114   -220       C  
ATOM    195  N   GLU A  25       3.883  15.942   9.843  1.00 27.48           N  
ANISOU  195  N   GLU A  25     3732   3764   2945      8    202   -516       N  
ATOM    196  CA  GLU A  25       3.572  15.030   8.756  1.00 25.78           C  
ANISOU  196  CA  GLU A  25     3526   3593   2678      8    205   -594       C  
ATOM    197  C   GLU A  25       4.517  13.852   8.633  1.00 36.23           C  
ANISOU  197  C   GLU A  25     4862   4866   4036     -2    250   -630       C  
ATOM    198  O   GLU A  25       4.068  12.777   8.244  1.00 31.39           O  
ANISOU  198  O   GLU A  25     4251   4261   3416    -23    250   -713       O  
ATOM    199  CB  GLU A  25       3.545  15.790   7.418  1.00 29.76           C  
ANISOU  199  CB  GLU A  25     4041   4181   3086     56    204   -579       C  
ATOM    200  CG  GLU A  25       2.428  16.814   7.408  1.00 42.68           C  
ANISOU  200  CG  GLU A  25     5662   5876   4679     70    157   -555       C  
ATOM    201  CD  GLU A  25       2.294  17.567   6.090  1.00 44.15           C  
ANISOU  201  CD  GLU A  25     5859   6152   4765    123    155   -537       C  
ATOM    202  OE1 GLU A  25       3.035  17.268   5.122  1.00 40.23           O  
ANISOU  202  OE1 GLU A  25     5382   5676   4226    149    189   -547       O  
ATOM    203  OE2 GLU A  25       1.438  18.472   6.046  1.00 42.54           O  
ANISOU  203  OE2 GLU A  25     5643   5996   4524    141    120   -508       O  
ATOM    204  N   ALA A  26       5.801  14.009   8.941  1.00 26.38           N  
ANISOU  204  N   ALA A  26     3624   3569   2831     11    290   -574       N  
ATOM    205  CA  ALA A  26       6.746  12.934   8.657  1.00 26.24           C  
ANISOU  205  CA  ALA A  26     3620   3512   2840      9    337   -606       C  
ATOM    206  C   ALA A  26       7.924  13.012   9.611  1.00 28.60           C  
ANISOU  206  C   ALA A  26     3915   3736   3215      8    367   -543       C  
ATOM    207  O   ALA A  26       8.248  14.100  10.109  1.00 27.40           O  
ANISOU  207  O   ALA A  26     3755   3580   3078     21    360   -471       O  
ATOM    208  CB  ALA A  26       7.261  13.004   7.205  1.00 32.22           C  
ANISOU  208  CB  ALA A  26     4397   4323   3522     46    365   -618       C  
ATOM    209  N   PRO A  27       8.599  11.884   9.860  1.00 32.55           N  
ANISOU  209  N   PRO A  27     4420   4180   3767     -4    403   -570       N  
ATOM    210  CA  PRO A  27       9.789  11.900  10.724  1.00 26.82           C  
ANISOU  210  CA  PRO A  27     3688   3391   3112      1    432   -512       C  
ATOM    211  C   PRO A  27      10.830  12.871  10.191  1.00 29.05           C  
ANISOU  211  C   PRO A  27     3972   3691   3373     37    456   -449       C  
ATOM    212  O   PRO A  27      11.039  12.993   8.982  1.00 28.62           O  
ANISOU  212  O   PRO A  27     3933   3681   3260     63    477   -461       O  
ATOM    213  CB  PRO A  27      10.296  10.446  10.657  1.00 25.96           C  
ANISOU  213  CB  PRO A  27     3588   3233   3041     -8    473   -562       C  
ATOM    214  CG  PRO A  27       9.069   9.638  10.325  1.00 32.99           C  
ANISOU  214  CG  PRO A  27     4483   4141   3908    -35    454   -647       C  
ATOM    215  CD  PRO A  27       8.281  10.524   9.377  1.00 32.94           C  
ANISOU  215  CD  PRO A  27     4480   4221   3815    -22    420   -658       C  
ATOM    216  N   GLN A  28      11.529  13.518  11.111  1.00 23.11           N  
ANISOU  216  N   GLN A  28     3204   2904   2675     39    458   -383       N  
ATOM    217  CA  GLN A  28      12.462  14.602  10.797  1.00 26.45           C  
ANISOU  217  CA  GLN A  28     3621   3336   3091     68    479   -317       C  
ATOM    218  C   GLN A  28      13.881  14.095  10.592  1.00 26.45           C  
ANISOU  218  C   GLN A  28     3620   3301   3127     84    532   -302       C  
ATOM    219  O   GLN A  28      14.874  14.722  10.977  1.00 24.93           O  
ANISOU  219  O   GLN A  28     3412   3086   2976     95    550   -245       O  
ATOM    220  CB  GLN A  28      12.391  15.654  11.903  1.00 25.00           C  
ANISOU  220  CB  GLN A  28     3416   3136   2946     58    449   -260       C  
ATOM    221  CG  GLN A  28      10.965  16.254  12.023  1.00 24.29           C  
ANISOU  221  CG  GLN A  28     3326   3084   2817     46    400   -271       C  
ATOM    222  CD  GLN A  28      10.573  17.106  10.824  1.00 25.58           C  
ANISOU  222  CD  GLN A  28     3502   3312   2903     74    400   -260       C  
ATOM    223  OE1 GLN A  28      11.091  18.210  10.647  1.00 26.29           O  
ANISOU  223  OE1 GLN A  28     3588   3409   2990     95    414   -202       O  
ATOM    224  NE2 GLN A  28       9.661  16.594   9.986  1.00 26.88           N  
ANISOU  224  NE2 GLN A  28     3682   3526   3006     75    385   -317       N  
ATOM    225  N   TYR A  29      14.011  12.925   9.974  1.00 24.93           N  
ANISOU  225  N   TYR A  29     3445   3104   2925     86    560   -357       N  
ATOM    226  CA  TYR A  29      15.329  12.314   9.831  1.00 25.85           C  
ANISOU  226  CA  TYR A  29     3560   3181   3080    102    613   -347       C  
ATOM    227  C   TYR A  29      16.234  13.058   8.859  1.00 32.73           C  
ANISOU  227  C   TYR A  29     4434   4080   3920    137    652   -307       C  
ATOM    228  O   TYR A  29      17.418  12.737   8.786  1.00 32.55           O  
ANISOU  228  O   TYR A  29     4405   4027   3936    152    696   -288       O  
ATOM    229  CB  TYR A  29      15.179  10.862   9.367  1.00 25.89           C  
ANISOU  229  CB  TYR A  29     3584   3171   3082     96    637   -420       C  
ATOM    230  CG  TYR A  29      14.432   9.964  10.317  1.00 26.79           C  
ANISOU  230  CG  TYR A  29     3694   3246   3239     63    614   -459       C  
ATOM    231  CD1 TYR A  29      14.465  10.186  11.693  1.00 25.25           C  
ANISOU  231  CD1 TYR A  29     3478   3011   3103     48    589   -417       C  
ATOM    232  CD2 TYR A  29      13.713   8.878   9.840  1.00 36.12           C  
ANISOU  232  CD2 TYR A  29     4893   4428   4402     47    619   -539       C  
ATOM    233  CE1 TYR A  29      13.761   9.341  12.575  1.00 27.62           C  
ANISOU  233  CE1 TYR A  29     3776   3274   3442     21    573   -448       C  
ATOM    234  CE2 TYR A  29      13.022   8.039  10.687  1.00 34.97           C  
ANISOU  234  CE2 TYR A  29     4744   4240   4301     16    605   -574       C  
ATOM    235  CZ  TYR A  29      13.059   8.262  12.050  1.00 36.70           C  
ANISOU  235  CZ  TYR A  29     4944   4421   4579      5    584   -525       C  
ATOM    236  OH  TYR A  29      12.363   7.405  12.857  1.00 36.49           O  
ANISOU  236  OH  TYR A  29     4916   4353   4595    -23    576   -557       O  
ATOM    237  N   TYR A  30      15.709  14.006   8.085  1.00 30.34           N  
ANISOU  237  N   TYR A  30     4142   3834   3550    152    640   -293       N  
ATOM    238  CA  TYR A  30      16.586  14.787   7.219  1.00 30.26           C  
ANISOU  238  CA  TYR A  30     4135   3847   3516    187    682   -246       C  
ATOM    239  C   TYR A  30      17.435  15.779   7.997  1.00 30.07           C  
ANISOU  239  C   TYR A  30     4082   3790   3554    187    689   -171       C  
ATOM    240  O   TYR A  30      18.387  16.319   7.432  1.00 35.27           O  
ANISOU  240  O   TYR A  30     4736   4450   4214    213    734   -129       O  
ATOM    241  CB  TYR A  30      15.769  15.535   6.178  1.00 28.41           C  
ANISOU  241  CB  TYR A  30     3921   3685   3190    208    670   -246       C  
ATOM    242  CG  TYR A  30      14.835  16.512   6.806  1.00 24.99           C  
ANISOU  242  CG  TYR A  30     3476   3267   2752    195    618   -219       C  
ATOM    243  CD1 TYR A  30      15.222  17.827   7.034  1.00 28.64           C  
ANISOU  243  CD1 TYR A  30     3925   3725   3233    207    625   -145       C  
ATOM    244  CD2 TYR A  30      13.557  16.123   7.175  1.00 29.40           C  
ANISOU  244  CD2 TYR A  30     4037   3841   3292    169    566   -268       C  
ATOM    245  CE1 TYR A  30      14.357  18.729   7.641  1.00 24.24           C  
ANISOU  245  CE1 TYR A  30     3357   3177   2676    194    580   -121       C  
ATOM    246  CE2 TYR A  30      12.684  17.013   7.769  1.00 27.16           C  
ANISOU  246  CE2 TYR A  30     3743   3571   3006    158    521   -243       C  
ATOM    247  CZ  TYR A  30      13.089  18.314   7.993  1.00 28.14           C  
ANISOU  247  CZ  TYR A  30     3855   3690   3148    172    528   -169       C  
ATOM    248  OH  TYR A  30      12.231  19.192   8.590  1.00 28.81           O  
ANISOU  248  OH  TYR A  30     3929   3784   3233    162    486   -146       O  
ATOM    249  N   LEU A  31      17.093  16.071   9.261  1.00 26.78           N  
ANISOU  249  N   LEU A  31     3643   3344   3187    160    647   -156       N  
ATOM    250  CA  LEU A  31      17.869  17.041  10.020  1.00 29.90           C  
ANISOU  250  CA  LEU A  31     4008   3711   3642    158    651    -93       C  
ATOM    251  C   LEU A  31      18.626  16.437  11.194  1.00 29.78           C  
ANISOU  251  C   LEU A  31     3966   3641   3709    142    649    -89       C  
ATOM    252  O   LEU A  31      19.398  17.157  11.842  1.00 27.92           O  
ANISOU  252  O   LEU A  31     3699   3383   3526    140    653    -43       O  
ATOM    253  CB  LEU A  31      16.971  18.188  10.510  1.00 29.89           C  
ANISOU  253  CB  LEU A  31     4000   3727   3629    146    607    -67       C  
ATOM    254  CG  LEU A  31      15.691  17.930  11.296  1.00 33.15           C  
ANISOU  254  CG  LEU A  31     4416   4144   4036    118    549   -100       C  
ATOM    255  CD1 LEU A  31      16.020  17.395  12.667  1.00 28.92           C  
ANISOU  255  CD1 LEU A  31     3858   3558   3573     94    531   -102       C  
ATOM    256  CD2 LEU A  31      14.870  19.227  11.444  1.00 34.56           C  
ANISOU  256  CD2 LEU A  31     4592   4348   4191    117    517    -69       C  
ATOM    257  N   ALA A  32      18.407  15.162  11.502  1.00 25.65           N  
ANISOU  257  N   ALA A  32     3451   3097   3197    131    644   -135       N  
ATOM    258  CA  ALA A  32      19.191  14.486  12.522  1.00 26.87           C  
ANISOU  258  CA  ALA A  32     3581   3202   3425    125    649   -127       C  
ATOM    259  C   ALA A  32      19.102  12.983  12.284  1.00 32.93           C  
ANISOU  259  C   ALA A  32     4369   3950   4192    126    669   -180       C  
ATOM    260  O   ALA A  32      18.107  12.477  11.749  1.00 30.58           O  
ANISOU  260  O   ALA A  32     4099   3673   3846    117    659   -231       O  
ATOM    261  CB  ALA A  32      18.712  14.841  13.938  1.00 27.14           C  
ANISOU  261  CB  ALA A  32     3595   3220   3496    101    598   -112       C  
ATOM    262  N  AGLU A  33      20.155  12.276  12.677  0.53 29.11           N  
ANISOU  262  N  AGLU A  33     3869   3428   3765    137    700   -170       N  
ATOM    263  N  BGLU A  33      20.151  12.273  12.689  0.47 29.11           N  
ANISOU  263  N  BGLU A  33     3869   3427   3765    137    699   -170       N  
ATOM    264  CA AGLU A  33      20.123  10.838  12.465  0.53 30.31           C  
ANISOU  264  CA AGLU A  33     4040   3553   3924    140    726   -218       C  
ATOM    265  CA BGLU A  33      20.160  10.832  12.520  0.47 30.34           C  
ANISOU  265  CA BGLU A  33     4043   3555   3931    140    726   -216       C  
ATOM    266  C  AGLU A  33      19.215  10.173  13.494  0.53 28.85           C  
ANISOU  266  C  AGLU A  33     3858   3343   3761    115    690   -243       C  
ATOM    267  C  BGLU A  33      19.191  10.183  13.503  0.47 28.84           C  
ANISOU  267  C  BGLU A  33     3857   3342   3760    114    689   -243       C  
ATOM    268  O  AGLU A  33      19.042  10.691  14.597  0.53 29.21           O  
ANISOU  268  O  AGLU A  33     3883   3381   3834    103    652   -211       O  
ATOM    269  O  BGLU A  33      18.947  10.721  14.582  0.47 29.26           O  
ANISOU  269  O  BGLU A  33     3891   3389   3837    101    649   -213       O  
ATOM    270  CB AGLU A  33      21.529  10.250  12.564  0.53 36.62           C  
ANISOU  270  CB AGLU A  33     4821   4317   4779    164    774   -196       C  
ATOM    271  CB BGLU A  33      21.563  10.272  12.740  0.47 36.46           C  
ANISOU  271  CB BGLU A  33     4796   4293   4766    163    770   -191       C  
ATOM    272  CG AGLU A  33      22.528  10.894  11.617  0.53 40.15           C  
ANISOU  272  CG AGLU A  33     5259   4783   5213    188    816   -167       C  
ATOM    273  CG BGLU A  33      22.589  10.801  11.758  0.47 40.27           C  
ANISOU  273  CG BGLU A  33     5272   4792   5237    188    815   -166       C  
ATOM    274  CD AGLU A  33      23.848  10.151  11.576  0.53 46.08           C  
ANISOU  274  CD AGLU A  33     5994   5500   6016    214    868   -155       C  
ATOM    275  CD BGLU A  33      22.365  10.292  10.352  0.47 44.50           C  
ANISOU  275  CD BGLU A  33     5845   5351   5714    201    853   -213       C  
ATOM    276  OE1AGLU A  33      23.876   8.961  11.947  0.53 50.20           O  
ANISOU  276  OE1AGLU A  33     6521   5985   6567    216    880   -181       O  
ATOM    277  OE1BGLU A  33      21.577   9.337  10.177  0.47 45.47           O  
ANISOU  277  OE1BGLU A  33     5994   5466   5815    189    850   -270       O  
ATOM    278  OE2AGLU A  33      24.858  10.760  11.171  0.53 55.91           O  
ANISOU  278  OE2AGLU A  33     7217   6752   7273    232    900   -118       O  
ATOM    279  OE2BGLU A  33      22.979  10.848   9.418  0.47 54.01           O  
ANISOU  279  OE2BGLU A  33     7051   6580   6892    222    889   -193       O  
ATOM    280  N   PRO A  34      18.632   9.024  13.148  1.00 28.57           N  
ANISOU  280  N   PRO A  34     3848   3292   3715    107    704   -301       N  
ATOM    281  CA  PRO A  34      17.682   8.363  14.056  1.00 29.81           C  
ANISOU  281  CA  PRO A  34     4010   3423   3895     82    676   -327       C  
ATOM    282  C   PRO A  34      18.246   8.089  15.435  1.00 30.44           C  
ANISOU  282  C   PRO A  34     4065   3458   4042     87    671   -284       C  
ATOM    283  O   PRO A  34      17.497   8.159  16.414  1.00 28.04           O  
ANISOU  283  O   PRO A  34     3757   3147   3752     68    634   -278       O  
ATOM    284  CB  PRO A  34      17.338   7.061  13.307  1.00 33.24           C  
ANISOU  284  CB  PRO A  34     4472   3838   4320     77    712   -397       C  
ATOM    285  CG  PRO A  34      17.576   7.380  11.848  1.00 31.56           C  
ANISOU  285  CG  PRO A  34     4275   3670   4047     93    736   -419       C  
ATOM    286  CD  PRO A  34      18.758   8.329  11.842  1.00 26.47           C  
ANISOU  286  CD  PRO A  34     3608   3036   3413    119    749   -350       C  
ATOM    287  N   TRP A  35      19.552   7.822  15.565  1.00 30.25           N  
ANISOU  287  N   TRP A  35     4023   3410   4060    114    707   -251       N  
ATOM    288  CA  TRP A  35      20.070   7.576  16.909  1.00 27.32           C  
ANISOU  288  CA  TRP A  35     3627   3006   3748    123    697   -209       C  
ATOM    289  C   TRP A  35      19.985   8.812  17.800  1.00 30.86           C  
ANISOU  289  C   TRP A  35     4048   3480   4198    114    645   -164       C  
ATOM    290  O   TRP A  35      19.921   8.669  19.029  1.00 25.37           O  
ANISOU  290  O   TRP A  35     3337   2767   3535    113    621   -140       O  
ATOM    291  CB  TRP A  35      21.500   7.049  16.839  1.00 32.21           C  
ANISOU  291  CB  TRP A  35     4227   3599   4412    157    744   -183       C  
ATOM    292  CG  TRP A  35      22.509   8.009  16.278  1.00 31.34           C  
ANISOU  292  CG  TRP A  35     4094   3518   4295    173    755   -150       C  
ATOM    293  CD1 TRP A  35      22.959   8.059  14.991  1.00 39.21           C  
ANISOU  293  CD1 TRP A  35     5103   4530   5266    185    796   -165       C  
ATOM    294  CD2 TRP A  35      23.201   9.033  16.986  1.00 36.40           C  
ANISOU  294  CD2 TRP A  35     4694   4175   4961    178    729    -97       C  
ATOM    295  NE1 TRP A  35      23.882   9.063  14.852  1.00 38.32           N  
ANISOU  295  NE1 TRP A  35     4960   4438   5162    197    801   -122       N  
ATOM    296  CE2 TRP A  35      24.053   9.678  16.061  1.00 34.97           C  
ANISOU  296  CE2 TRP A  35     4501   4014   4772    191    759    -82       C  
ATOM    297  CE3 TRP A  35      23.182   9.477  18.310  1.00 35.18           C  
ANISOU  297  CE3 TRP A  35     4511   4021   4834    172    684    -64       C  
ATOM    298  CZ2 TRP A  35      24.882  10.734  16.426  1.00 42.15           C  
ANISOU  298  CZ2 TRP A  35     5370   4939   5707    196    747    -37       C  
ATOM    299  CZ3 TRP A  35      24.010  10.538  18.668  1.00 43.16           C  
ANISOU  299  CZ3 TRP A  35     5481   5051   5866    177    668    -24       C  
ATOM    300  CH2 TRP A  35      24.841  11.150  17.733  1.00 38.61           C  
ANISOU  300  CH2 TRP A  35     4892   4491   5288    187    700    -11       C  
ATOM    301  N   GLN A  36      19.959  10.025  17.211  1.00 26.19           N  
ANISOU  301  N   GLN A  36     3452   2930   3571    108    630   -152       N  
ATOM    302  CA  GLN A  36      19.804  11.234  18.013  1.00 25.94           C  
ANISOU  302  CA  GLN A  36     3396   2918   3541     97    583   -116       C  
ATOM    303  C   GLN A  36      18.386  11.348  18.567  1.00 31.67           C  
ANISOU  303  C   GLN A  36     4138   3651   4243     70    539   -137       C  
ATOM    304  O   GLN A  36      18.188  11.719  19.734  1.00 22.57           O  
ANISOU  304  O   GLN A  36     2968   2496   3111     62    503   -113       O  
ATOM    305  CB  GLN A  36      20.157  12.463  17.157  1.00 26.91           C  
ANISOU  305  CB  GLN A  36     3512   3076   3637    100    589    -97       C  
ATOM    306  CG  GLN A  36      21.590  12.469  16.598  1.00 33.15           C  
ANISOU  306  CG  GLN A  36     4282   3860   4453    126    636    -74       C  
ATOM    307  CD  GLN A  36      21.770  13.581  15.569  1.00 30.26           C  
ANISOU  307  CD  GLN A  36     3917   3525   4053    130    651    -59       C  
ATOM    308  OE1 GLN A  36      21.951  13.317  14.388  1.00 36.10           O  
ANISOU  308  OE1 GLN A  36     4679   4277   4763    144    691    -75       O  
ATOM    309  NE2 GLN A  36      21.674  14.826  16.017  1.00 45.19           N  
ANISOU  309  NE2 GLN A  36     5788   5432   5950    118    621    -28       N  
ATOM    310  N   PHE A  37      17.377  11.032  17.745  1.00 22.91           N  
ANISOU  310  N   PHE A  37     3059   2555   3089     56    541   -183       N  
ATOM    311  CA  PHE A  37      16.013  10.986  18.268  1.00 22.92           C  
ANISOU  311  CA  PHE A  37     3074   2561   3075     30    503   -207       C  
ATOM    312  C   PHE A  37      15.893   9.946  19.366  1.00 21.98           C  
ANISOU  312  C   PHE A  37     2953   2397   3000     27    504   -208       C  
ATOM    313  O   PHE A  37      15.179  10.154  20.356  1.00 23.41           O  
ANISOU  313  O   PHE A  37     3130   2576   3189     12    470   -199       O  
ATOM    314  CB  PHE A  37      15.017  10.676  17.137  1.00 22.17           C  
ANISOU  314  CB  PHE A  37     3007   2488   2927     16    507   -263       C  
ATOM    315  CG  PHE A  37      14.891  11.815  16.155  1.00 22.91           C  
ANISOU  315  CG  PHE A  37     3105   2633   2967     22    498   -256       C  
ATOM    316  CD1 PHE A  37      14.102  12.909  16.460  1.00 22.59           C  
ANISOU  316  CD1 PHE A  37     3059   2623   2903      9    455   -239       C  
ATOM    317  CD2 PHE A  37      15.626  11.824  14.976  1.00 30.79           C  
ANISOU  317  CD2 PHE A  37     4110   3647   3940     43    537   -260       C  
ATOM    318  CE1 PHE A  37      14.013  13.992  15.541  1.00 22.10           C  
ANISOU  318  CE1 PHE A  37     3000   2605   2791     19    452   -225       C  
ATOM    319  CE2 PHE A  37      15.561  12.895  14.090  1.00 23.16           C  
ANISOU  319  CE2 PHE A  37     3148   2727   2924     53    534   -244       C  
ATOM    320  CZ  PHE A  37      14.769  13.960  14.367  1.00 22.75           C  
ANISOU  320  CZ  PHE A  37     3091   2703   2849     42    493   -226       C  
ATOM    321  N  ASER A  38      16.576   8.810  19.210  0.57 22.37           N  
ANISOU  321  N  ASER A  38     3007   2411   3081     44    549   -218       N  
ATOM    322  N  BSER A  38      16.575   8.809  19.210  0.44 22.41           N  
ANISOU  322  N  BSER A  38     3013   2416   3087     44    549   -218       N  
ATOM    323  CA ASER A  38      16.469   7.789  20.247  0.57 24.65           C  
ANISOU  323  CA ASER A  38     3296   2654   3414     46    557   -214       C  
ATOM    324  CA BSER A  38      16.491   7.776  20.239  0.44 24.66           C  
ANISOU  324  CA BSER A  38     3298   2656   3417     47    558   -214       C  
ATOM    325  C  ASER A  38      17.046   8.278  21.576  0.57 25.06           C  
ANISOU  325  C  ASER A  38     3319   2705   3498     60    530   -156       C  
ATOM    326  C  BSER A  38      17.037   8.287  21.572  0.44 25.04           C  
ANISOU  326  C  BSER A  38     3317   2703   3495     60    530   -156       C  
ATOM    327  O  ASER A  38      16.558   7.904  22.654  0.57 25.66           O  
ANISOU  327  O  ASER A  38     3395   2761   3594     57    515   -145       O  
ATOM    328  O  BSER A  38      16.512   7.955  22.645  0.44 25.64           O  
ANISOU  328  O  BSER A  38     3393   2761   3589     56    513   -146       O  
ATOM    329  CB ASER A  38      17.171   6.509  19.788  0.57 24.35           C  
ANISOU  329  CB ASER A  38     3269   2575   3407     66    615   -231       C  
ATOM    330  CB BSER A  38      17.240   6.526  19.774  0.44 24.31           C  
ANISOU  330  CB BSER A  38     3262   2570   3403     68    616   -230       C  
ATOM    331  OG ASER A  38      16.733   5.419  20.580  0.57 23.17           O  
ANISOU  331  OG ASER A  38     3130   2379   3296     64    629   -239       O  
ATOM    332  OG BSER A  38      16.652   6.008  18.594  0.44 22.86           O  
ANISOU  332  OG BSER A  38     3107   2389   3191     53    640   -291       O  
ATOM    333  N   MET A  39      18.086   9.102  21.525  1.00 23.37           N  
ANISOU  333  N   MET A  39     3079   2513   3289     77    526   -120       N  
ATOM    334  CA  MET A  39      18.653   9.641  22.751  1.00 26.29           C  
ANISOU  334  CA  MET A  39     3416   2888   3685     89    496    -73       C  
ATOM    335  C   MET A  39      17.661  10.559  23.462  1.00 28.18           C  
ANISOU  335  C   MET A  39     3654   3151   3902     64    444    -70       C  
ATOM    336  O   MET A  39      17.574  10.548  24.692  1.00 25.58           O  
ANISOU  336  O   MET A  39     3312   2817   3589     69    418    -46       O  
ATOM    337  CB  MET A  39      19.955  10.389  22.433  1.00 21.56           C  
ANISOU  337  CB  MET A  39     2785   2308   3099    106    504    -44       C  
ATOM    338  CG  MET A  39      21.119   9.453  22.199  1.00 32.16           C  
ANISOU  338  CG  MET A  39     4117   3625   4478    138    550    -34       C  
ATOM    339  SD  MET A  39      22.565  10.446  21.806  1.00 52.65           S  
ANISOU  339  SD  MET A  39     6669   6244   7090    154    559     -1       S  
ATOM    340  CE  MET A  39      22.971  11.090  23.429  1.00 41.52           C  
ANISOU  340  CE  MET A  39     5215   4852   5710    160    507     38       C  
ATOM    341  N   LEU A  40      16.911  11.366  22.705  1.00 23.05           N  
ANISOU  341  N   LEU A  40     3017   2528   3211     42    428    -91       N  
ATOM    342  CA  LEU A  40      15.853  12.164  23.327  1.00 20.47           C  
ANISOU  342  CA  LEU A  40     2692   2221   2864     19    382    -91       C  
ATOM    343  C   LEU A  40      14.806  11.275  23.974  1.00 20.43           C  
ANISOU  343  C   LEU A  40     2706   2193   2862      7    377   -111       C  
ATOM    344  O   LEU A  40      14.310  11.577  25.059  1.00 20.53           O  
ANISOU  344  O   LEU A  40     2713   2209   2879      0    345    -95       O  
ATOM    345  CB  LEU A  40      15.192  13.074  22.294  1.00 23.17           C  
ANISOU  345  CB  LEU A  40     3046   2596   3160      2    372   -110       C  
ATOM    346  CG  LEU A  40      16.077  14.100  21.584  1.00 23.60           C  
ANISOU  346  CG  LEU A  40     3084   2673   3209     12    381    -87       C  
ATOM    347  CD1 LEU A  40      15.208  14.796  20.545  1.00 25.60           C  
ANISOU  347  CD1 LEU A  40     3357   2958   3411      0    375   -106       C  
ATOM    348  CD2 LEU A  40      16.602  15.102  22.568  1.00 28.44           C  
ANISOU  348  CD2 LEU A  40     3665   3293   3848     12    353    -50       C  
ATOM    349  N   ALA A  41      14.438  10.185  23.319  1.00 21.28           N  
ANISOU  349  N   ALA A  41     2837   2278   2969      3    410   -148       N  
ATOM    350  CA  ALA A  41      13.402   9.330  23.887  1.00 20.73           C  
ANISOU  350  CA  ALA A  41     2785   2182   2910    -12    411   -170       C  
ATOM    351  C   ALA A  41      13.897   8.637  25.150  1.00 22.10           C  
ANISOU  351  C   ALA A  41     2949   2321   3126     10    420   -134       C  
ATOM    352  O   ALA A  41      13.148   8.506  26.117  1.00 21.46           O  
ANISOU  352  O   ALA A  41     2872   2232   3051      2    403   -126       O  
ATOM    353  CB  ALA A  41      12.938   8.299  22.860  1.00 24.37           C  
ANISOU  353  CB  ALA A  41     3271   2622   3366    -23    447   -224       C  
ATOM    354  N   ALA A  42      15.144   8.155  25.143  1.00 22.76           N  
ANISOU  354  N   ALA A  42     3021   2388   3238     40    449   -110       N  
ATOM    355  CA  ALA A  42      15.681   7.511  26.336  1.00 21.17           C  
ANISOU  355  CA  ALA A  42     2808   2161   3073     69    458    -70       C  
ATOM    356  C   ALA A  42      15.701   8.489  27.501  1.00 26.19           C  
ANISOU  356  C   ALA A  42     3421   2828   3700     72    408    -33       C  
ATOM    357  O   ALA A  42      15.384   8.129  28.640  1.00 20.81           O  
ANISOU  357  O   ALA A  42     2741   2135   3030     82    400    -10       O  
ATOM    358  CB  ALA A  42      17.081   6.989  26.058  1.00 22.54           C  
ANISOU  358  CB  ALA A  42     2968   2320   3276    104    494    -49       C  
ATOM    359  N   TYR A  43      16.093   9.732  27.227  1.00 20.60           N  
ANISOU  359  N   TYR A  43     2693   2159   2973     66    378    -26       N  
ATOM    360  CA  TYR A  43      16.122  10.755  28.259  1.00 23.00           C  
ANISOU  360  CA  TYR A  43     2974   2494   3270     65    331      1       C  
ATOM    361  C   TYR A  43      14.722  11.033  28.803  1.00 24.15           C  
ANISOU  361  C   TYR A  43     3137   2645   3393     39    303    -13       C  
ATOM    362  O   TYR A  43      14.527  11.123  30.020  1.00 24.22           O  
ANISOU  362  O   TYR A  43     3140   2659   3405     47    279     10       O  
ATOM    363  CB  TYR A  43      16.764  12.006  27.664  1.00 23.01           C  
ANISOU  363  CB  TYR A  43     2952   2528   3262     58    314      4       C  
ATOM    364  CG  TYR A  43      16.723  13.263  28.497  1.00 22.79           C  
ANISOU  364  CG  TYR A  43     2900   2532   3226     49    267     19       C  
ATOM    365  CD1 TYR A  43      17.612  13.456  29.542  1.00 28.66           C  
ANISOU  365  CD1 TYR A  43     3610   3288   3990     70    247     48       C  
ATOM    366  CD2 TYR A  43      15.873  14.287  28.167  1.00 21.14           C  
ANISOU  366  CD2 TYR A  43     2701   2342   2990     20    244      4       C  
ATOM    367  CE1 TYR A  43      17.607  14.627  30.273  1.00 29.31           C  
ANISOU  367  CE1 TYR A  43     3669   3400   4066     60    205     55       C  
ATOM    368  CE2 TYR A  43      15.859  15.477  28.901  1.00 21.68           C  
ANISOU  368  CE2 TYR A  43     2747   2435   3056     11    205     15       C  
ATOM    369  CZ  TYR A  43      16.736  15.631  29.935  1.00 28.94           C  
ANISOU  369  CZ  TYR A  43     3634   3366   3997     29    186     38       C  
ATOM    370  OH  TYR A  43      16.740  16.800  30.652  1.00 26.41           O  
ANISOU  370  OH  TYR A  43     3292   3069   3675     18    149     41       O  
ATOM    371  N   MET A  44      13.727  11.163  27.922  1.00 20.77           N  
ANISOU  371  N   MET A  44     2732   2219   2942     10    305    -50       N  
ATOM    372  CA  MET A  44      12.375  11.442  28.415  1.00 19.90           C  
ANISOU  372  CA  MET A  44     2634   2114   2812    -14    279    -63       C  
ATOM    373  C   MET A  44      11.799  10.269  29.195  1.00 22.11           C  
ANISOU  373  C   MET A  44     2930   2358   3113    -10    299    -62       C  
ATOM    374  O   MET A  44      11.018  10.465  30.127  1.00 21.24           O  
ANISOU  374  O   MET A  44     2822   2250   2996    -17    277    -53       O  
ATOM    375  CB  MET A  44      11.424  11.787  27.258  1.00 21.76           C  
ANISOU  375  CB  MET A  44     2887   2364   3018    -43    277   -104       C  
ATOM    376  CG  MET A  44      11.724  13.167  26.590  1.00 19.40           C  
ANISOU  376  CG  MET A  44     2574   2103   2693    -48    254   -100       C  
ATOM    377  SD  MET A  44      11.962  14.513  27.754  1.00 21.31           S  
ANISOU  377  SD  MET A  44     2791   2370   2937    -46    210    -63       S  
ATOM    378  CE  MET A  44      10.397  14.535  28.663  1.00 21.93           C  
ANISOU  378  CE  MET A  44     2882   2447   3001    -66    183    -74       C  
ATOM    379  N   PHE A  45      12.128   9.046  28.806  1.00 20.17           N  
ANISOU  379  N   PHE A  45     2697   2075   2893      2    344    -71       N  
ATOM    380  CA  PHE A  45      11.624   7.907  29.557  1.00 20.39           C  
ANISOU  380  CA  PHE A  45     2739   2061   2946      8    371    -66       C  
ATOM    381  C   PHE A  45      12.188   7.909  30.978  1.00 22.22           C  
ANISOU  381  C   PHE A  45     2957   2296   3190     42    359    -12       C  
ATOM    382  O   PHE A  45      11.456   7.664  31.948  1.00 24.16           O  
ANISOU  382  O   PHE A  45     3211   2531   3438     42    355      2       O  
ATOM    383  CB  PHE A  45      11.990   6.616  28.818  1.00 20.84           C  
ANISOU  383  CB  PHE A  45     2811   2073   3034     17    428    -86       C  
ATOM    384  CG  PHE A  45      11.391   5.388  29.425  1.00 21.53           C  
ANISOU  384  CG  PHE A  45     2916   2108   3155     19    466    -86       C  
ATOM    385  CD1 PHE A  45      10.021   5.240  29.509  1.00 25.75           C  
ANISOU  385  CD1 PHE A  45     3464   2631   3686    -15    464   -118       C  
ATOM    386  CD2 PHE A  45      12.213   4.355  29.874  1.00 26.86           C  
ANISOU  386  CD2 PHE A  45     3593   2744   3869     56    509    -53       C  
ATOM    387  CE1 PHE A  45       9.466   4.093  30.050  1.00 30.38           C  
ANISOU  387  CE1 PHE A  45     4067   3165   4311    -15    506   -118       C  
ATOM    388  CE2 PHE A  45      11.665   3.210  30.414  1.00 29.13           C  
ANISOU  388  CE2 PHE A  45     3898   2977   4192     60    552    -49       C  
ATOM    389  CZ  PHE A  45      10.293   3.076  30.504  1.00 29.33           C  
ANISOU  389  CZ  PHE A  45     3939   2988   4218     23    552    -82       C  
ATOM    390  N   LEU A  46      13.479   8.229  31.112  1.00 23.07           N  
ANISOU  390  N   LEU A  46     3041   2422   3303     71    351     18       N  
ATOM    391  CA  LEU A  46      14.084   8.380  32.431  1.00 25.40           C  
ANISOU  391  CA  LEU A  46     3315   2734   3600    105    330     66       C  
ATOM    392  C   LEU A  46      13.367   9.455  33.241  1.00 24.93           C  
ANISOU  392  C   LEU A  46     3250   2711   3512     88    280     69       C  
ATOM    393  O   LEU A  46      13.042   9.241  34.414  1.00 23.51           O  
ANISOU  393  O   LEU A  46     3074   2532   3329    104    271     95       O  
ATOM    394  CB  LEU A  46      15.562   8.721  32.294  1.00 23.08           C  
ANISOU  394  CB  LEU A  46     2990   2463   3316    132    323     88       C  
ATOM    395  CG  LEU A  46      16.316   8.805  33.628  1.00 33.03           C  
ANISOU  395  CG  LEU A  46     4223   3748   4578    172    300    134       C  
ATOM    396  CD1 LEU A  46      16.351   7.435  34.242  1.00 33.48           C  
ANISOU  396  CD1 LEU A  46     4295   3767   4657    208    340    164       C  
ATOM    397  CD2 LEU A  46      17.724   9.384  33.489  1.00 37.95           C  
ANISOU  397  CD2 LEU A  46     4806   4404   5211    192    284    148       C  
ATOM    398  N   LEU A  47      13.117  10.624  32.638  1.00 24.11           N  
ANISOU  398  N   LEU A  47     3138   2636   3385     58    249     45       N  
ATOM    399  CA  LEU A  47      12.481  11.703  33.399  1.00 22.04           C  
ANISOU  399  CA  LEU A  47     2870   2406   3098     43    204     47       C  
ATOM    400  C   LEU A  47      11.097  11.284  33.881  1.00 26.83           C  
ANISOU  400  C   LEU A  47     3502   2995   3698     27    209     38       C  
ATOM    401  O   LEU A  47      10.700  11.634  34.999  1.00 25.58           O  
ANISOU  401  O   LEU A  47     3341   2851   3526     33    185     55       O  
ATOM    402  CB  LEU A  47      12.375  12.988  32.569  1.00 20.93           C  
ANISOU  402  CB  LEU A  47     2720   2293   2939     15    179     24       C  
ATOM    403  CG  LEU A  47      13.653  13.754  32.234  1.00 25.03           C  
ANISOU  403  CG  LEU A  47     3209   2835   3466     25    168     34       C  
ATOM    404  CD1 LEU A  47      13.350  15.088  31.541  1.00 22.19           C  
ANISOU  404  CD1 LEU A  47     2844   2498   3089     -3    147     15       C  
ATOM    405  CD2 LEU A  47      14.442  13.957  33.465  1.00 29.59           C  
ANISOU  405  CD2 LEU A  47     3759   3433   4051     51    144     62       C  
ATOM    406  N   ILE A  48      10.340  10.551  33.049  1.00 24.17           N  
ANISOU  406  N   ILE A  48     3188   2627   3369      6    240      7       N  
ATOM    407  CA  ILE A  48       9.002  10.110  33.454  1.00 22.51           C  
ANISOU  407  CA  ILE A  48     2998   2396   3159    -13    249     -6       C  
ATOM    408  C   ILE A  48       9.095   9.081  34.570  1.00 21.93           C  
ANISOU  408  C   ILE A  48     2933   2293   3107     17    277     30       C  
ATOM    409  O   ILE A  48       8.394   9.183  35.584  1.00 26.61           O  
ANISOU  409  O   ILE A  48     3530   2889   3691     19    266     46       O  
ATOM    410  CB  ILE A  48       8.216   9.554  32.252  1.00 25.94           C  
ANISOU  410  CB  ILE A  48     3449   2807   3600    -44    276    -54       C  
ATOM    411  CG1 ILE A  48       7.904  10.669  31.249  1.00 23.93           C  
ANISOU  411  CG1 ILE A  48     3188   2589   3314    -70    245    -85       C  
ATOM    412  CG2 ILE A  48       6.936   8.907  32.738  1.00 30.44           C  
ANISOU  412  CG2 ILE A  48     4035   3350   4182    -62    293    -67       C  
ATOM    413  CD1 ILE A  48       7.452  10.118  29.868  1.00 25.81           C  
ANISOU  413  CD1 ILE A  48     3439   2815   3551    -93    270   -135       C  
ATOM    414  N   MET A  49       9.984   8.083  34.410  1.00 24.30           N  
ANISOU  414  N   MET A  49     3234   2563   3435     46    315     46       N  
ATOM    415  CA  MET A  49      10.088   6.985  35.380  1.00 26.35           C  
ANISOU  415  CA  MET A  49     3504   2789   3718     80    351     85       C  
ATOM    416  C   MET A  49      10.664   7.448  36.716  1.00 28.01           C  
ANISOU  416  C   MET A  49     3697   3036   3909    118    319    135       C  
ATOM    417  O   MET A  49      10.378   6.844  37.756  1.00 28.70           O  
ANISOU  417  O   MET A  49     3796   3108   4000    143    337    169       O  
ATOM    418  CB  MET A  49      10.959   5.848  34.815  1.00 21.53           C  
ANISOU  418  CB  MET A  49     2898   2138   3145    104    401     91       C  
ATOM    419  CG  MET A  49      10.346   5.150  33.596  1.00 23.04           C  
ANISOU  419  CG  MET A  49     3108   2288   3358     68    441     38       C  
ATOM    420  SD  MET A  49       8.732   4.391  33.947  1.00 37.64           S  
ANISOU  420  SD  MET A  49     4982   4091   5229     38    473     16       S  
ATOM    421  CE  MET A  49       9.228   3.129  35.111  1.00 45.82           C  
ANISOU  421  CE  MET A  49     6029   5079   6303     91    527     78       C  
ATOM    422  N   LEU A  50      11.488   8.488  36.713  1.00 27.52           N  
ANISOU  422  N   LEU A  50     3610   3022   3826    124    275    138       N  
ATOM    423  CA  LEU A  50      11.920   9.082  37.971  1.00 28.55           C  
ANISOU  423  CA  LEU A  50     3721   3196   3933    154    236    173       C  
ATOM    424  C   LEU A  50      10.935  10.128  38.457  1.00 23.30           C  
ANISOU  424  C   LEU A  50     3058   2559   3237    125    197    157       C  
ATOM    425  O   LEU A  50      10.672  10.221  39.659  1.00 24.69           O  
ANISOU  425  O   LEU A  50     3235   2753   3393    145    182    183       O  
ATOM    426  CB  LEU A  50      13.296   9.733  37.814  1.00 31.02           C  
ANISOU  426  CB  LEU A  50     3998   3546   4242    172    208    180       C  
ATOM    427  CG  LEU A  50      14.424   8.821  37.336  1.00 43.32           C  
ANISOU  427  CG  LEU A  50     5547   5082   5830    204    244    198       C  
ATOM    428  CD1 LEU A  50      15.741   9.592  37.241  1.00 42.10           C  
ANISOU  428  CD1 LEU A  50     5351   4970   5674    218    212    203       C  
ATOM    429  CD2 LEU A  50      14.564   7.608  38.231  1.00 39.47           C  
ANISOU  429  CD2 LEU A  50     5071   4571   5356    251    278    244       C  
ATOM    430  N   GLY A  51      10.389  10.919  37.535  1.00 22.12           N  
ANISOU  430  N   GLY A  51     2909   2415   3080     82    181    116       N  
ATOM    431  CA  GLY A  51       9.558  12.043  37.941  1.00 27.16           C  
ANISOU  431  CA  GLY A  51     3546   3083   3692     57    142    102       C  
ATOM    432  C   GLY A  51       8.244  11.617  38.558  1.00 31.50           C  
ANISOU  432  C   GLY A  51     4119   3613   4236     48    156    103       C  
ATOM    433  O   GLY A  51       7.758  12.248  39.499  1.00 23.38           O  
ANISOU  433  O   GLY A  51     3089   2609   3184     49    130    111       O  
ATOM    434  N   PHE A  52       7.621  10.579  38.016  1.00 21.57           N  
ANISOU  434  N   PHE A  52     2882   2310   3003     35    200     91       N  
ATOM    435  CA  PHE A  52       6.368  10.138  38.621  1.00 25.89           C  
ANISOU  435  CA  PHE A  52     3448   2834   3553     24    219     92       C  
ATOM    436  C   PHE A  52       6.548   9.664  40.066  1.00 24.48           C  
ANISOU  436  C   PHE A  52     3275   2657   3368     67    229    142       C  
ATOM    437  O   PHE A  52       5.866  10.206  40.950  1.00 22.70           O  
ANISOU  437  O   PHE A  52     3053   2453   3120     66    209    150       O  
ATOM    438  CB  PHE A  52       5.711   9.080  37.725  1.00 30.06           C  
ANISOU  438  CB  PHE A  52     3994   3312   4115      0    267     63       C  
ATOM    439  CG  PHE A  52       4.678   8.245  38.430  1.00 37.29           C  
ANISOU  439  CG  PHE A  52     4928   4191   5050     -3    304     73       C  
ATOM    440  CD1 PHE A  52       3.639   8.843  39.133  1.00 36.79           C  
ANISOU  440  CD1 PHE A  52     4866   4144   4967    -17    285     72       C  
ATOM    441  CD2 PHE A  52       4.737   6.859  38.374  1.00 49.14           C  
ANISOU  441  CD2 PHE A  52     6444   5636   6592      9    363     82       C  
ATOM    442  CE1 PHE A  52       2.684   8.075  39.783  1.00 39.34           C  
ANISOU  442  CE1 PHE A  52     5205   4432   5312    -20    324     83       C  
ATOM    443  CE2 PHE A  52       3.789   6.078  39.016  1.00 43.89           C  
ANISOU  443  CE2 PHE A  52     5794   4931   5951      6    405     93       C  
ATOM    444  CZ  PHE A  52       2.761   6.684  39.725  1.00 46.52           C  
ANISOU  444  CZ  PHE A  52     6128   5283   6264     -9    385     94       C  
ATOM    445  N   PRO A  53       7.423   8.711  40.389  1.00 25.06           N  
ANISOU  445  N   PRO A  53     3351   2712   3459    108    260    178       N  
ATOM    446  CA  PRO A  53       7.487   8.273  41.795  1.00 27.28           C  
ANISOU  446  CA  PRO A  53     3639   2999   3729    153    270    230       C  
ATOM    447  C   PRO A  53       7.966   9.360  42.757  1.00 29.55           C  
ANISOU  447  C   PRO A  53     3906   3351   3970    175    213    246       C  
ATOM    448  O   PRO A  53       7.402   9.494  43.848  1.00 30.65           O  
ANISOU  448  O   PRO A  53     4054   3506   4084    190    207    268       O  
ATOM    449  CB  PRO A  53       8.458   7.069  41.768  1.00 28.92           C  
ANISOU  449  CB  PRO A  53     3849   3175   3965    196    314    265       C  
ATOM    450  CG  PRO A  53       8.667   6.717  40.334  1.00 32.28           C  
ANISOU  450  CG  PRO A  53     4275   3567   4424    167    336    226       C  
ATOM    451  CD  PRO A  53       8.355   7.954  39.530  1.00 30.72           C  
ANISOU  451  CD  PRO A  53     4064   3402   4206    120    289    177       C  
ATOM    452  N  AILE A  54       8.979  10.151  42.395  0.52 24.03           N  
ANISOU  452  N  AILE A  54     3180   2690   3261    177    173    234       N  
ATOM    453  N  BILE A  54       8.983  10.140  42.385  0.48 24.03           N  
ANISOU  453  N  BILE A  54     3181   2690   3261    177    174    234       N  
ATOM    454  CA AILE A  54       9.527  11.084  43.377  0.52 21.47           C  
ANISOU  454  CA AILE A  54     2833   2426   2898    199    122    246       C  
ATOM    455  CA BILE A  54       9.545  11.103  43.329  0.48 21.49           C  
ANISOU  455  CA BILE A  54     2836   2429   2902    198    122    244       C  
ATOM    456  C  AILE A  54       8.523  12.192  43.692  0.52 22.50           C  
ANISOU  456  C  AILE A  54     2968   2580   3002    166     89    218       C  
ATOM    457  C  BILE A  54       8.516  12.171  43.684  0.48 22.51           C  
ANISOU  457  C  BILE A  54     2969   2580   3004    166     90    218       C  
ATOM    458  O  AILE A  54       8.417  12.637  44.839  0.52 24.88           O  
ANISOU  458  O  AILE A  54     3265   2918   3269    186     64    232       O  
ATOM    459  O  BILE A  54       8.397  12.580  44.845  0.48 24.87           O  
ANISOU  459  O  BILE A  54     3266   2915   3270    187     66    234       O  
ATOM    460  CB AILE A  54      10.889  11.642  42.917  0.52 27.57           C  
ANISOU  460  CB AILE A  54     3571   3230   3674    207     91    236       C  
ATOM    461  CB BILE A  54      10.829  11.731  42.759  0.48 27.41           C  
ANISOU  461  CB BILE A  54     3551   3208   3655    200     90    230       C  
ATOM    462  CG1AILE A  54      11.619  12.297  44.092  0.52 25.89           C  
ANISOU  462  CG1AILE A  54     3331   3079   3425    241     44    253       C  
ATOM    463  CG1BILE A  54      11.885  10.653  42.485  0.48 23.31           C  
ANISOU  463  CG1BILE A  54     3025   2669   3162    237    123    259       C  
ATOM    464  CG2AILE A  54      10.750  12.643  41.789  0.52 20.54           C  
ANISOU  464  CG2AILE A  54     2672   2342   2792    156     71    189       C  
ATOM    465  CG2BILE A  54      11.369  12.788  43.718  0.48 26.11           C  
ANISOU  465  CG2BILE A  54     3359   3107   3456    215     35    231       C  
ATOM    466  CD1AILE A  54      13.050  12.693  43.766  0.52 27.93           C  
ANISOU  466  CD1AILE A  54     3549   3368   3693    254     18    247       C  
ATOM    467  CD1BILE A  54      13.192  11.229  41.996  0.48 29.94           C  
ANISOU  467  CD1BILE A  54     3828   3539   4009    242     95    249       C  
ATOM    468  N   ASN A  55       7.769  12.652  42.691  1.00 21.73           N  
ANISOU  468  N   ASN A  55     2876   2463   2918    116     89    178       N  
ATOM    469  CA  ASN A  55       6.749  13.662  42.957  1.00 22.33           C  
ANISOU  469  CA  ASN A  55     2956   2557   2973     86     63    154       C  
ATOM    470  C   ASN A  55       5.519  13.073  43.643  1.00 26.78           C  
ANISOU  470  C   ASN A  55     3544   3097   3532     87     92    168       C  
ATOM    471  O   ASN A  55       4.912  13.735  44.487  1.00 21.40           O  
ANISOU  471  O   ASN A  55     2866   2441   2825     86     71    168       O  
ATOM    472  CB  ASN A  55       6.350  14.361  41.665  1.00 21.34           C  
ANISOU  472  CB  ASN A  55     2826   2422   2859     40     54    112       C  
ATOM    473  CG  ASN A  55       7.390  15.334  41.211  1.00 20.34           C  
ANISOU  473  CG  ASN A  55     2672   2325   2730     36     20     98       C  
ATOM    474  OD1 ASN A  55       7.574  16.374  41.841  1.00 21.29           O  
ANISOU  474  OD1 ASN A  55     2777   2481   2830     36    -17     92       O  
ATOM    475  ND2 ASN A  55       8.094  15.008  40.103  1.00 21.86           N  
ANISOU  475  ND2 ASN A  55     2859   2502   2946     31     36     90       N  
ATOM    476  N   PHE A  56       5.121  11.846  43.288  1.00 24.15           N  
ANISOU  476  N   PHE A  56     3230   2714   3230     87    143    178       N  
ATOM    477  CA  PHE A  56       3.981  11.243  43.982  1.00 23.73           C  
ANISOU  477  CA  PHE A  56     3200   2636   3181     87    177    193       C  
ATOM    478  C   PHE A  56       4.304  10.981  45.452  1.00 25.66           C  
ANISOU  478  C   PHE A  56     3450   2903   3397    140    179    243       C  
ATOM    479  O   PHE A  56       3.450  11.184  46.330  1.00 23.98           O  
ANISOU  479  O   PHE A  56     3249   2699   3164    143    181    254       O  
ATOM    480  CB  PHE A  56       3.534   9.948  43.290  1.00 24.35           C  
ANISOU  480  CB  PHE A  56     3295   2652   3306     74    236    189       C  
ATOM    481  CG  PHE A  56       2.448   9.259  44.043  1.00 32.08           C  
ANISOU  481  CG  PHE A  56     4293   3598   4296     77    278    209       C  
ATOM    482  CD1 PHE A  56       1.167   9.754  44.028  1.00 39.43           C  
ANISOU  482  CD1 PHE A  56     5228   4530   5226     39    273    181       C  
ATOM    483  CD2 PHE A  56       2.734   8.176  44.852  1.00 34.87           C  
ANISOU  483  CD2 PHE A  56     4662   3926   4660    121    324    260       C  
ATOM    484  CE1 PHE A  56       0.172   9.149  44.787  1.00 29.09           C  
ANISOU  484  CE1 PHE A  56     3933   3191   3928     42    314    201       C  
ATOM    485  CE2 PHE A  56       1.745   7.574  45.585  1.00 38.95           C  
ANISOU  485  CE2 PHE A  56     5198   4412   5190    125    368    282       C  
ATOM    486  CZ  PHE A  56       0.466   8.066  45.549  1.00 28.92           C  
ANISOU  486  CZ  PHE A  56     3929   3141   3920     84    363    251       C  
ATOM    487  N  ALEU A  57       5.523  10.521  45.739  0.45 24.78           N  
ANISOU  487  N  ALEU A  57     3330   2804   3282    184    180    276       N  
ATOM    488  N  BLEU A  57       5.523  10.518  45.737  0.55 24.75           N  
ANISOU  488  N  BLEU A  57     3326   2800   3278    184    180    276       N  
ATOM    489  CA ALEU A  57       5.906  10.284  47.126  0.45 25.19           C  
ANISOU  489  CA ALEU A  57     3385   2886   3299    241    178    326       C  
ATOM    490  CA BLEU A  57       5.916  10.292  47.124  0.55 25.16           C  
ANISOU  490  CA BLEU A  57     3381   2883   3295    241    178    325       C  
ATOM    491  C  ALEU A  57       5.935  11.586  47.917  0.45 26.23           C  
ANISOU  491  C  ALEU A  57     3501   3083   3381    243    119    312       C  
ATOM    492  C  BLEU A  57       5.909  11.594  47.908  0.55 26.22           C  
ANISOU  492  C  BLEU A  57     3500   3081   3380    242    119    311       C  
ATOM    493  O  ALEU A  57       5.599  11.602  49.107  0.45 27.40           O  
ANISOU  493  O  ALEU A  57     3661   3257   3494    274    118    339       O  
ATOM    494  O  BLEU A  57       5.526  11.616  49.085  0.55 27.38           O  
ANISOU  494  O  BLEU A  57     3658   3252   3492    271    119    338       O  
ATOM    495  CB ALEU A  57       7.263   9.580  47.190  0.45 28.76           C  
ANISOU  495  CB ALEU A  57     3826   3345   3757    290    186    361       C  
ATOM    496  CB BLEU A  57       7.302   9.649  47.189  0.55 28.77           C  
ANISOU  496  CB BLEU A  57     3825   3350   3757    289    182    360       C  
ATOM    497  CG ALEU A  57       7.309   8.127  46.696  0.45 28.62           C  
ANISOU  497  CG ALEU A  57     3825   3260   3787    303    254    386       C  
ATOM    498  CG BLEU A  57       7.773   9.179  48.563  0.55 30.01           C  
ANISOU  498  CG BLEU A  57     3985   3538   3878    358    187    418       C  
ATOM    499  CD1ALEU A  57       8.729   7.596  46.682  0.45 29.74           C  
ANISOU  499  CD1ALEU A  57     3951   3414   3935    351    256    418       C  
ATOM    500  CD1BLEU A  57       6.767   8.200  49.138  0.55 31.23           C  
ANISOU  500  CD1BLEU A  57     4174   3647   4044    374    249    456       C  
ATOM    501  CD2ALEU A  57       6.436   7.251  47.579  0.45 35.62           C  
ANISOU  501  CD2ALEU A  57     4742   4115   4678    327    307    428       C  
ATOM    502  CD2BLEU A  57       9.145   8.534  48.464  0.55 38.54           C  
ANISOU  502  CD2BLEU A  57     5048   4626   4968    405    192    450       C  
ATOM    503  N   THR A  58       6.352  12.690  47.282  1.00 24.47           N  
ANISOU  503  N   THR A  58     3256   2888   3156    212     72    269       N  
ATOM    504  CA  THR A  58       6.360  13.970  47.986  1.00 21.18           C  
ANISOU  504  CA  THR A  58     2823   2526   2698    208     19    249       C  
ATOM    505  C   THR A  58       4.937  14.387  48.342  1.00 25.44           C  
ANISOU  505  C   THR A  58     3382   3056   3226    182     26    235       C  
ATOM    506  O   THR A  58       4.671  14.846  49.460  1.00 24.57           O  
ANISOU  506  O   THR A  58     3276   2984   3077    202      8    243       O  
ATOM    507  CB  THR A  58       7.042  15.058  47.133  1.00 25.62           C  
ANISOU  507  CB  THR A  58     3356   3107   3270    176    -23    206       C  
ATOM    508  OG1 THR A  58       8.410  14.691  46.901  1.00 30.28           O  
ANISOU  508  OG1 THR A  58     3924   3710   3871    203    -29    220       O  
ATOM    509  CG2 THR A  58       7.032  16.381  47.863  1.00 27.44           C  
ANISOU  509  CG2 THR A  58     3571   3389   3467    170    -72    180       C  
ATOM    510  N   LEU A  59       4.011  14.221  47.397  1.00 25.54           N  
ANISOU  510  N   LEU A  59     3407   3024   3273    139     52    213       N  
ATOM    511  CA  LEU A  59       2.608  14.539  47.656  1.00 28.04           C  
ANISOU  511  CA  LEU A  59     3739   3329   3584    114     62    201       C  
ATOM    512  C   LEU A  59       2.054  13.668  48.771  1.00 28.28           C  
ANISOU  512  C   LEU A  59     3793   3350   3603    148    101    244       C  
ATOM    513  O   LEU A  59       1.375  14.154  49.687  1.00 34.66           O  
ANISOU  513  O   LEU A  59     4609   4180   4380    155     94    248       O  
ATOM    514  CB  LEU A  59       1.807  14.342  46.371  1.00 25.30           C  
ANISOU  514  CB  LEU A  59     3396   2938   3278     66     84    170       C  
ATOM    515  CG  LEU A  59       0.294  14.538  46.294  1.00 39.47           C  
ANISOU  515  CG  LEU A  59     5201   4713   5081     32     99    150       C  
ATOM    516  CD1 LEU A  59      -0.017  14.738  44.829  1.00 33.27           C  
ANISOU  516  CD1 LEU A  59     4408   3909   4326    -13     96    110       C  
ATOM    517  CD2 LEU A  59      -0.460  13.332  46.803  1.00 44.99           C  
ANISOU  517  CD2 LEU A  59     5922   5374   5800     43    155    179       C  
ATOM    518  N   TYR A  60       2.333  12.374  48.696  1.00 25.08           N  
ANISOU  518  N   TYR A  60     3399   2907   3222    172    147    278       N  
ATOM    519  CA  TYR A  60       1.746  11.418  49.622  1.00 27.13           C  
ANISOU  519  CA  TYR A  60     3683   3144   3480    204    198    324       C  
ATOM    520  C   TYR A  60       2.265  11.632  51.033  1.00 30.96           C  
ANISOU  520  C   TYR A  60     4170   3684   3908    261    178    363       C  
ATOM    521  O   TYR A  60       1.496  11.605  52.001  1.00 30.70           O  
ANISOU  521  O   TYR A  60     4154   3658   3850    278    195    385       O  
ATOM    522  CB  TYR A  60       2.056  10.003  49.150  1.00 27.30           C  
ANISOU  522  CB  TYR A  60     3716   3110   3547    218    254    352       C  
ATOM    523  CG  TYR A  60       1.369   8.920  49.966  1.00 33.78           C  
ANISOU  523  CG  TYR A  60     4563   3892   4379    246    320    400       C  
ATOM    524  CD1 TYR A  60       1.899   8.488  51.179  1.00 46.53           C  
ANISOU  524  CD1 TYR A  60     6188   5532   5958    313    332    461       C  
ATOM    525  CD2 TYR A  60       0.194   8.330  49.515  1.00 43.50           C  
ANISOU  525  CD2 TYR A  60     5807   5064   5659    207    371    385       C  
ATOM    526  CE1 TYR A  60       1.273   7.501  51.929  1.00 44.38           C  
ANISOU  526  CE1 TYR A  60     5942   5222   5697    342    399    512       C  
ATOM    527  CE2 TYR A  60      -0.435   7.335  50.257  1.00 44.57           C  
ANISOU  527  CE2 TYR A  60     5965   5157   5812    231    438    431       C  
ATOM    528  CZ  TYR A  60       0.105   6.933  51.460  1.00 48.20           C  
ANISOU  528  CZ  TYR A  60     6439   5640   6236    299    454    496       C  
ATOM    529  OH  TYR A  60      -0.521   5.951  52.198  1.00 64.75           O  
ANISOU  529  OH  TYR A  60     8559   7693   8350    327    526    547       O  
ATOM    530  N   VAL A  61       3.576  11.830  51.167  1.00 25.56           N  
ANISOU  530  N   VAL A  61     3467   3042   3202    293    141    371       N  
ATOM    531  CA  VAL A  61       4.158  12.047  52.492  1.00 29.29           C  
ANISOU  531  CA  VAL A  61     3936   3577   3615    351    115    402       C  
ATOM    532  C   VAL A  61       3.595  13.320  53.114  1.00 28.14           C  
ANISOU  532  C   VAL A  61     3787   3478   3428    334     72    369       C  
ATOM    533  O   VAL A  61       3.287  13.363  54.316  1.00 31.20           O  
ANISOU  533  O   VAL A  61     4187   3899   3768    370     74    394       O  
ATOM    534  CB  VAL A  61       5.698  12.086  52.406  1.00 31.66           C  
ANISOU  534  CB  VAL A  61     4208   3916   3904    383     79    408       C  
ATOM    535  CG1 VAL A  61       6.302  12.538  53.754  1.00 34.58           C  
ANISOU  535  CG1 VAL A  61     4566   4366   4205    437     37    426       C  
ATOM    536  CG2 VAL A  61       6.236  10.707  52.066  1.00 26.44           C  
ANISOU  536  CG2 VAL A  61     3555   3212   3278    415    129    453       C  
ATOM    537  N   THR A  62       3.455  14.375  52.314  1.00 25.27           N  
ANISOU  537  N   THR A  62     3406   3116   3080    280     36    312       N  
ATOM    538  CA  THR A  62       2.972  15.647  52.847  1.00 28.65           C  
ANISOU  538  CA  THR A  62     3828   3583   3473    263     -4    277       C  
ATOM    539  C   THR A  62       1.531  15.533  53.338  1.00 33.80           C  
ANISOU  539  C   THR A  62     4508   4213   4121    253     32    286       C  
ATOM    540  O   THR A  62       1.177  16.060  54.403  1.00 32.08           O  
ANISOU  540  O   THR A  62     4297   4035   3857    273     18    288       O  
ATOM    541  CB  THR A  62       3.077  16.729  51.771  1.00 30.47           C  
ANISOU  541  CB  THR A  62     4036   3810   3730    208    -39    220       C  
ATOM    542  OG1 THR A  62       4.437  16.814  51.328  1.00 29.88           O  
ANISOU  542  OG1 THR A  62     3936   3755   3664    217    -68    213       O  
ATOM    543  CG2 THR A  62       2.641  18.085  52.333  1.00 28.22           C  
ANISOU  543  CG2 THR A  62     3745   3562   3414    191    -78    183       C  
ATOM    544  N   VAL A  63       0.681  14.857  52.567  1.00 31.03           N  
ANISOU  544  N   VAL A  63     4170   3801   3818    222     78    289       N  
ATOM    545  CA  VAL A  63      -0.719  14.723  52.958  1.00 38.51           C  
ANISOU  545  CA  VAL A  63     5138   4723   4770    209    115    295       C  
ATOM    546  C   VAL A  63      -0.845  13.851  54.202  1.00 32.77           C  
ANISOU  546  C   VAL A  63     4435   4002   4013    266    156    354       C  
ATOM    547  O   VAL A  63      -1.682  14.107  55.072  1.00 41.14           O  
ANISOU  547  O   VAL A  63     5509   5075   5046    275    168    363       O  
ATOM    548  CB  VAL A  63      -1.541  14.182  51.777  1.00 37.73           C  
ANISOU  548  CB  VAL A  63     5042   4560   4733    161    153    278       C  
ATOM    549  CG1 VAL A  63      -2.939  13.772  52.243  1.00 47.03           C  
ANISOU  549  CG1 VAL A  63     6238   5707   5923    152    202    291       C  
ATOM    550  CG2 VAL A  63      -1.615  15.253  50.673  1.00 37.23           C  
ANISOU  550  CG2 VAL A  63     4957   4501   4686    110    111    221       C  
ATOM    551  N   GLN A  64       0.003  12.823  54.317  1.00 33.20           N  
ANISOU  551  N   GLN A  64     4494   4048   4072    307    179    398       N  
ATOM    552  CA  GLN A  64      -0.086  11.885  55.429  1.00 40.86           C  
ANISOU  552  CA  GLN A  64     5488   5019   5018    366    226    463       C  
ATOM    553  C   GLN A  64       0.315  12.506  56.765  1.00 48.67           C  
ANISOU  553  C   GLN A  64     6478   6086   5928    418    188    478       C  
ATOM    554  O   GLN A  64      -0.204  12.086  57.802  1.00 38.00           O  
ANISOU  554  O   GLN A  64     5151   4743   4546    458    225    523       O  
ATOM    555  CB  GLN A  64       0.784  10.651  55.164  1.00 35.70           C  
ANISOU  555  CB  GLN A  64     4839   4336   4392    402    261    507       C  
ATOM    556  CG  GLN A  64       0.500   9.501  56.124  1.00 54.46           C  
ANISOU  556  CG  GLN A  64     7243   6690   6759    458    328    581       C  
ATOM    557  CD  GLN A  64       1.423   8.323  55.911  1.00 54.12           C  
ANISOU  557  CD  GLN A  64     7203   6620   6742    500    363    628       C  
ATOM    558  OE1 GLN A  64       2.602   8.499  55.620  1.00 68.23           O  
ANISOU  558  OE1 GLN A  64     8969   8440   8517    516    321    621       O  
ATOM    559  NE2 GLN A  64       0.891   7.112  56.044  1.00 63.22           N  
ANISOU  559  NE2 GLN A  64     8380   7707   7934    516    445    676       N  
ATOM    560  N   HIS A  65       1.245  13.473  56.785  1.00 41.40           N  
ANISOU  560  N   HIS A  65     5532   5226   4974    419    119    443       N  
ATOM    561  CA  HIS A  65       1.801  13.984  58.043  1.00 37.41           C  
ANISOU  561  CA  HIS A  65     5022   4800   4390    472     79    452       C  
ATOM    562  C   HIS A  65       1.327  15.408  58.308  1.00 43.16           C  
ANISOU  562  C   HIS A  65     5741   5566   5090    438     32    394       C  
ATOM    563  O   HIS A  65       1.787  16.354  57.658  1.00 36.90           O  
ANISOU  563  O   HIS A  65     4922   4788   4312    399    -18    339       O  
ATOM    564  CB  HIS A  65       3.327  13.915  58.023  1.00 37.55           C  
ANISOU  564  CB  HIS A  65     5013   4864   4391    507     37    457       C  
ATOM    565  CG  HIS A  65       3.855  12.522  57.925  1.00 41.65           C  
ANISOU  565  CG  HIS A  65     5542   5353   4931    551     84    521       C  
ATOM    566  ND1 HIS A  65       4.065  11.727  59.030  1.00 47.67           N  
ANISOU  566  ND1 HIS A  65     6322   6143   5648    627    111    588       N  
ATOM    567  CD2 HIS A  65       4.214  11.778  56.850  1.00 36.78           C  
ANISOU  567  CD2 HIS A  65     4920   4677   4376    533    111    528       C  
ATOM    568  CE1 HIS A  65       4.533  10.553  58.642  1.00 51.83           C  
ANISOU  568  CE1 HIS A  65     6854   6627   6211    654    156    636       C  
ATOM    569  NE2 HIS A  65       4.622  10.552  57.324  1.00 39.59           N  
ANISOU  569  NE2 HIS A  65     5291   5024   4729    596    157    598       N  
ATOM    570  N   LYS A  66       0.456  15.566  59.314  1.00 41.04           N  
ANISOU  570  N   LYS A  66     5495   5316   4781    458     51    408       N  
ATOM    571  CA  LYS A  66      -0.130  16.872  59.599  1.00 41.04           C  
ANISOU  571  CA  LYS A  66     5490   5345   4758    427     16    354       C  
ATOM    572  C   LYS A  66       0.891  17.866  60.142  1.00 38.03           C  
ANISOU  572  C   LYS A  66     5084   5043   4324    445    -56    314       C  
ATOM    573  O   LYS A  66       0.640  19.075  60.100  1.00 42.47           O  
ANISOU  573  O   LYS A  66     5634   5622   4882    408    -92    256       O  
ATOM    574  CB  LYS A  66      -1.296  16.730  60.584  1.00 46.63           C  
ANISOU  574  CB  LYS A  66     6230   6054   5435    448     58    381       C  
ATOM    575  N   LYS A  67       2.040  17.397  60.628  1.00 39.18           N  
ANISOU  575  N   LYS A  67     5218   5237   4433    498    -76    342       N  
ATOM    576  CA  LYS A  67       3.098  18.319  61.024  1.00 42.86           C  
ANISOU  576  CA  LYS A  67     5651   5777   4857    509   -147    296       C  
ATOM    577  C   LYS A  67       3.626  19.142  59.854  1.00 48.55           C  
ANISOU  577  C   LYS A  67     6338   6477   5633    448   -186    236       C  
ATOM    578  O   LYS A  67       4.224  20.197  60.077  1.00 46.22           O  
ANISOU  578  O   LYS A  67     6014   6231   5317    436   -241    181       O  
ATOM    579  CB  LYS A  67       4.262  17.553  61.665  1.00 47.97           C  
ANISOU  579  CB  LYS A  67     6288   6480   5460    581   -161    340       C  
ATOM    580  CG  LYS A  67       4.915  16.524  60.769  1.00 49.49           C  
ANISOU  580  CG  LYS A  67     6473   6627   5706    586   -136    379       C  
ATOM    581  N   LEU A  68       3.428  18.691  58.613  1.00 36.32           N  
ANISOU  581  N   LEU A  68     4790   4856   4153    408   -155    244       N  
ATOM    582  CA  LEU A  68       4.085  19.326  57.465  1.00 35.41           C  
ANISOU  582  CA  LEU A  68     4643   4724   4088    359   -187    198       C  
ATOM    583  C   LEU A  68       3.177  20.407  56.876  1.00 36.61           C  
ANISOU  583  C   LEU A  68     4796   4844   4270    297   -192    147       C  
ATOM    584  O   LEU A  68       2.641  20.287  55.782  1.00 36.36           O  
ANISOU  584  O   LEU A  68     4770   4753   4292    255   -166    143       O  
ATOM    585  CB  LEU A  68       4.446  18.282  56.413  1.00 28.59           C  
ANISOU  585  CB  LEU A  68     3779   3806   3277    354   -154    231       C  
ATOM    586  CG  LEU A  68       5.433  17.181  56.832  1.00 34.93           C  
ANISOU  586  CG  LEU A  68     4579   4633   4061    416   -146    284       C  
ATOM    587  CD1 LEU A  68       5.640  16.184  55.683  1.00 35.00           C  
ANISOU  587  CD1 LEU A  68     4590   4576   4131    403   -106    310       C  
ATOM    588  CD2 LEU A  68       6.754  17.773  57.260  1.00 42.41           C  
ANISOU  588  CD2 LEU A  68     5486   5652   4974    440   -207    258       C  
ATOM    589  N   ARG A  69       3.034  21.507  57.618  1.00 31.27           N  
ANISOU  589  N   ARG A  69     4113   4211   3557    293   -226    105       N  
ATOM    590  CA  ARG A  69       2.115  22.557  57.198  1.00 33.54           C  
ANISOU  590  CA  ARG A  69     4404   4471   3871    242   -226     61       C  
ATOM    591  C   ARG A  69       2.753  23.944  57.284  1.00 35.43           C  
ANISOU  591  C   ARG A  69     4612   4745   4106    218   -279     -4       C  
ATOM    592  O   ARG A  69       2.058  24.946  57.409  1.00 36.43           O  
ANISOU  592  O   ARG A  69     4742   4867   4234    191   -284    -42       O  
ATOM    593  CB  ARG A  69       0.818  22.491  58.002  1.00 40.66           C  
ANISOU  593  CB  ARG A  69     5338   5369   4743    253   -194     77       C  
ATOM    594  CG  ARG A  69       0.019  21.165  57.839  1.00 41.18           C  
ANISOU  594  CG  ARG A  69     5434   5388   4826    266   -133    137       C  
ATOM    595  CD  ARG A  69      -0.597  21.006  56.437  1.00 45.41           C  
ANISOU  595  CD  ARG A  69     5968   5853   5432    214   -107    132       C  
ATOM    596  NE  ARG A  69      -1.381  19.779  56.313  1.00 50.34           N  
ANISOU  596  NE  ARG A  69     6617   6432   6077    222    -49    179       N  
ATOM    597  CZ  ARG A  69      -0.884  18.600  55.962  1.00 48.23           C  
ANISOU  597  CZ  ARG A  69     6354   6141   5830    240    -23    218       C  
ATOM    598  NH1 ARG A  69       0.403  18.443  55.688  1.00 42.71           N  
ANISOU  598  NH1 ARG A  69     5636   5462   5131    256    -50    220       N  
ATOM    599  NH2 ARG A  69      -1.694  17.549  55.887  1.00 41.14           N  
ANISOU  599  NH2 ARG A  69     5477   5196   4956    243     35    256       N  
ATOM    600  N   THR A  70       4.075  24.025  57.198  1.00 30.50           N  
ANISOU  600  N   THR A  70     3954   4153   3481    228   -315    -18       N  
ATOM    601  CA  THR A  70       4.709  25.323  57.017  1.00 29.71           C  
ANISOU  601  CA  THR A  70     3820   4071   3397    195   -358    -83       C  
ATOM    602  C   THR A  70       4.508  25.801  55.578  1.00 29.78           C  
ANISOU  602  C   THR A  70     3822   4017   3477    140   -344    -99       C  
ATOM    603  O   THR A  70       4.159  25.013  54.698  1.00 30.73           O  
ANISOU  603  O   THR A  70     3956   4089   3628    131   -310    -62       O  
ATOM    604  CB  THR A  70       6.202  25.227  57.326  1.00 31.96           C  
ANISOU  604  CB  THR A  70     4067   4410   3666    222   -399    -94       C  
ATOM    605  OG1 THR A  70       6.832  24.454  56.300  1.00 36.52           O  
ANISOU  605  OG1 THR A  70     4634   4954   4287    218   -384    -62       O  
ATOM    606  CG2 THR A  70       6.456  24.572  58.713  1.00 36.10           C  
ANISOU  606  CG2 THR A  70     4599   5004   4114    288   -412    -67       C  
ATOM    607  N   PRO A  71       4.699  27.103  55.316  1.00 31.22           N  
ANISOU  607  N   PRO A  71     3982   4197   3685    102   -368   -155       N  
ATOM    608  CA  PRO A  71       4.638  27.586  53.927  1.00 32.49           C  
ANISOU  608  CA  PRO A  71     4133   4302   3909     55   -354   -166       C  
ATOM    609  C   PRO A  71       5.552  26.819  52.975  1.00 28.73           C  
ANISOU  609  C   PRO A  71     3642   3810   3465     56   -349   -140       C  
ATOM    610  O   PRO A  71       5.155  26.534  51.839  1.00 29.46           O  
ANISOU  610  O   PRO A  71     3745   3852   3595     34   -321   -121       O  
ATOM    611  CB  PRO A  71       5.057  29.060  54.069  1.00 36.67           C  
ANISOU  611  CB  PRO A  71     4634   4844   4455     26   -384   -230       C  
ATOM    612  CG  PRO A  71       4.529  29.442  55.467  1.00 32.49           C  
ANISOU  612  CG  PRO A  71     4117   4357   3870     47   -398   -253       C  
ATOM    613  CD  PRO A  71       4.781  28.213  56.294  1.00 34.77           C  
ANISOU  613  CD  PRO A  71     4417   4689   4104    100   -400   -210       C  
ATOM    614  N   LEU A  72       6.759  26.462  53.415  1.00 28.83           N  
ANISOU  614  N   LEU A  72     3628   3866   3462     84   -375   -139       N  
ATOM    615  CA  LEU A  72       7.630  25.673  52.557  1.00 27.92           C  
ANISOU  615  CA  LEU A  72     3498   3735   3376     90   -367   -112       C  
ATOM    616  C   LEU A  72       6.976  24.341  52.212  1.00 28.56           C  
ANISOU  616  C   LEU A  72     3614   3782   3454    108   -325    -55       C  
ATOM    617  O   LEU A  72       7.029  23.907  51.064  1.00 26.88           O  
ANISOU  617  O   LEU A  72     3405   3526   3282     91   -301    -38       O  
ATOM    618  CB  LEU A  72       8.986  25.456  53.222  1.00 28.13           C  
ANISOU  618  CB  LEU A  72     3488   3819   3380    124   -403   -118       C  
ATOM    619  CG  LEU A  72       9.968  24.598  52.419  1.00 29.57           C  
ANISOU  619  CG  LEU A  72     3654   3990   3592    135   -394    -88       C  
ATOM    620  CD1 LEU A  72      10.561  25.379  51.262  1.00 32.28           C  
ANISOU  620  CD1 LEU A  72     3968   4302   3995     90   -395   -119       C  
ATOM    621  CD2 LEU A  72      11.061  24.027  53.328  1.00 34.09           C  
ANISOU  621  CD2 LEU A  72     4199   4627   4128    187   -423    -75       C  
ATOM    622  N   ASN A  73       6.350  23.678  53.195  1.00 26.53           N  
ANISOU  622  N   ASN A  73     3385   3544   3153    144   -313    -25       N  
ATOM    623  CA  ASN A  73       5.699  22.396  52.911  1.00 28.57           C  
ANISOU  623  CA  ASN A  73     3676   3765   3417    160   -267     27       C  
ATOM    624  C   ASN A  73       4.578  22.552  51.894  1.00 26.98           C  
ANISOU  624  C   ASN A  73     3494   3504   3254    115   -236     22       C  
ATOM    625  O   ASN A  73       4.394  21.686  51.029  1.00 26.18           O  
ANISOU  625  O   ASN A  73     3403   3360   3182    108   -203     48       O  
ATOM    626  CB  ASN A  73       5.128  21.766  54.186  1.00 30.64           C  
ANISOU  626  CB  ASN A  73     3964   4053   3625    204   -254     61       C  
ATOM    627  CG  ASN A  73       6.171  21.551  55.270  1.00 33.64           C  
ANISOU  627  CG  ASN A  73     4325   4500   3956    257   -285     70       C  
ATOM    628  OD1 ASN A  73       5.918  21.851  56.437  1.00 31.25           O  
ANISOU  628  OD1 ASN A  73     4030   4244   3600    284   -301     64       O  
ATOM    629  ND2 ASN A  73       7.349  21.028  54.894  1.00 27.44           N  
ANISOU  629  ND2 ASN A  73     3515   3725   3185    275   -295     85       N  
ATOM    630  N   TYR A  74       3.773  23.617  52.019  1.00 27.20           N  
ANISOU  630  N   TYR A  74     3525   3529   3280     88   -244    -11       N  
ATOM    631  CA  TYR A  74       2.691  23.842  51.064  1.00 24.37           C  
ANISOU  631  CA  TYR A  74     3182   3122   2955     49   -219    -16       C  
ATOM    632  C   TYR A  74       3.223  24.092  49.664  1.00 22.30           C  
ANISOU  632  C   TYR A  74     2902   2832   2739     18   -220    -29       C  
ATOM    633  O   TYR A  74       2.630  23.636  48.686  1.00 23.99           O  
ANISOU  633  O   TYR A  74     3128   3006   2979     -1   -192    -18       O  
ATOM    634  CB  TYR A  74       1.837  25.041  51.471  1.00 25.32           C  
ANISOU  634  CB  TYR A  74     3305   3247   3066     29   -229    -50       C  
ATOM    635  CG  TYR A  74       0.783  24.697  52.483  1.00 33.11           C  
ANISOU  635  CG  TYR A  74     4319   4243   4019     49   -210    -32       C  
ATOM    636  CD1 TYR A  74      -0.346  23.981  52.117  1.00 43.35           C  
ANISOU  636  CD1 TYR A  74     5639   5503   5330     41   -170     -6       C  
ATOM    637  CD2 TYR A  74       0.906  25.100  53.797  1.00 40.24           C  
ANISOU  637  CD2 TYR A  74     5224   5192   4875     75   -230    -44       C  
ATOM    638  CE1 TYR A  74      -1.323  23.669  53.044  1.00 50.66           C  
ANISOU  638  CE1 TYR A  74     6587   6433   6228     59   -147     12       C  
ATOM    639  CE2 TYR A  74      -0.057  24.794  54.734  1.00 45.61           C  
ANISOU  639  CE2 TYR A  74     5928   5880   5520     97   -208    -25       C  
ATOM    640  CZ  TYR A  74      -1.170  24.082  54.351  1.00 49.87           C  
ANISOU  640  CZ  TYR A  74     6490   6378   6079     88   -165      4       C  
ATOM    641  OH  TYR A  74      -2.129  23.782  55.286  1.00 50.46           O  
ANISOU  641  OH  TYR A  74     6589   6459   6124    109   -139     24       O  
ATOM    642  N   ILE A  75       4.283  24.897  49.550  1.00 25.73           N  
ANISOU  642  N   ILE A  75     3307   3286   3183     10   -250    -57       N  
ATOM    643  CA  ILE A  75       4.823  25.239  48.237  1.00 25.10           C  
ANISOU  643  CA  ILE A  75     3210   3180   3147    -18   -248    -68       C  
ATOM    644  C   ILE A  75       5.420  24.002  47.559  1.00 21.31           C  
ANISOU  644  C   ILE A  75     2732   2685   2682     -4   -228    -36       C  
ATOM    645  O   ILE A  75       5.261  23.802  46.345  1.00 25.97           O  
ANISOU  645  O   ILE A  75     3326   3241   3302    -24   -208    -32       O  
ATOM    646  CB  ILE A  75       5.854  26.376  48.392  1.00 30.19           C  
ANISOU  646  CB  ILE A  75     3820   3849   3804    -29   -281   -106       C  
ATOM    647  CG1 ILE A  75       5.149  27.676  48.781  1.00 35.35           C  
ANISOU  647  CG1 ILE A  75     4474   4503   4455    -51   -291   -141       C  
ATOM    648  CG2 ILE A  75       6.661  26.583  47.101  1.00 26.58           C  
ANISOU  648  CG2 ILE A  75     3341   3367   3390    -50   -275   -110       C  
ATOM    649  CD1 ILE A  75       4.283  28.215  47.687  1.00 41.50           C  
ANISOU  649  CD1 ILE A  75     5264   5238   5264    -82   -268   -143       C  
ATOM    650  N   LEU A  76       6.100  23.144  48.333  1.00 25.78           N  
ANISOU  650  N   LEU A  76     3293   3276   3224     35   -233    -13       N  
ATOM    651  CA  LEU A  76       6.656  21.932  47.742  1.00 24.00           C  
ANISOU  651  CA  LEU A  76     3071   3032   3015     52   -210     19       C  
ATOM    652  C   LEU A  76       5.562  20.951  47.359  1.00 25.90           C  
ANISOU  652  C   LEU A  76     3345   3232   3262     49   -168     45       C  
ATOM    653  O   LEU A  76       5.706  20.224  46.373  1.00 24.01           O  
ANISOU  653  O   LEU A  76     3111   2961   3051     42   -143     56       O  
ATOM    654  CB  LEU A  76       7.654  21.276  48.701  1.00 23.79           C  
ANISOU  654  CB  LEU A  76     3031   3046   2963     99   -224     42       C  
ATOM    655  CG  LEU A  76       9.138  21.635  48.470  1.00 24.56           C  
ANISOU  655  CG  LEU A  76     3087   3170   3076    104   -252     26       C  
ATOM    656  CD1 LEU A  76       9.680  21.008  47.189  1.00 28.73           C  
ANISOU  656  CD1 LEU A  76     3610   3661   3644     95   -226     40       C  
ATOM    657  CD2 LEU A  76       9.328  23.142  48.426  1.00 30.23           C  
ANISOU  657  CD2 LEU A  76     3779   3902   3804     70   -284    -23       C  
ATOM    658  N   LEU A  77       4.466  20.917  48.127  1.00 23.69           N  
ANISOU  658  N   LEU A  77     3088   2954   2959     53   -159     51       N  
ATOM    659  CA  LEU A  77       3.304  20.137  47.714  1.00 22.00           C  
ANISOU  659  CA  LEU A  77     2900   2699   2758     41   -119     66       C  
ATOM    660  C   LEU A  77       2.749  20.645  46.396  1.00 21.46           C  
ANISOU  660  C   LEU A  77     2831   2601   2721     -2   -113     40       C  
ATOM    661  O   LEU A  77       2.429  19.850  45.493  1.00 23.97           O  
ANISOU  661  O   LEU A  77     3158   2885   3063    -15    -84     47       O  
ATOM    662  CB  LEU A  77       2.225  20.192  48.811  1.00 22.40           C  
ANISOU  662  CB  LEU A  77     2972   2759   2780     52   -110     74       C  
ATOM    663  CG  LEU A  77       0.902  19.479  48.524  1.00 29.03           C  
ANISOU  663  CG  LEU A  77     3835   3559   3637     36    -68     86       C  
ATOM    664  CD1 LEU A  77       1.096  18.000  48.152  1.00 33.13           C  
ANISOU  664  CD1 LEU A  77     4366   4044   4179     51    -28    118       C  
ATOM    665  CD2 LEU A  77      -0.005  19.598  49.742  1.00 33.68           C  
ANISOU  665  CD2 LEU A  77     4441   4163   4195     52    -60     97       C  
ATOM    666  N   ASN A  78       2.640  21.972  46.258  1.00 24.19           N  
ANISOU  666  N   ASN A  78     3164   2960   3066    -25   -140     10       N  
ATOM    667  CA  ASN A  78       2.173  22.553  44.999  1.00 22.80           C  
ANISOU  667  CA  ASN A  78     2985   2761   2916    -60   -136    -10       C  
ATOM    668  C   ASN A  78       3.105  22.190  43.842  1.00 22.96           C  
ANISOU  668  C   ASN A  78     2994   2769   2961    -65   -130     -8       C  
ATOM    669  O   ASN A  78       2.640  21.829  42.757  1.00 22.15           O  
ANISOU  669  O   ASN A  78     2900   2642   2876    -83   -110    -11       O  
ATOM    670  CB  ASN A  78       2.066  24.074  45.132  1.00 25.52           C  
ANISOU  670  CB  ASN A  78     3316   3121   3258    -77   -162    -38       C  
ATOM    671  CG  ASN A  78       1.381  24.722  43.910  1.00 24.04           C  
ANISOU  671  CG  ASN A  78     3129   2912   3092   -107   -154    -52       C  
ATOM    672  OD1 ASN A  78       0.385  24.214  43.419  1.00 33.57           O  
ANISOU  672  OD1 ASN A  78     4350   4102   4303   -117   -135    -47       O  
ATOM    673  ND2 ASN A  78       1.924  25.836  43.448  1.00 30.01           N  
ANISOU  673  ND2 ASN A  78     3868   3671   3862   -120   -169    -69       N  
ATOM    674  N   LEU A  79       4.425  22.234  44.066  1.00 22.83           N  
ANISOU  674  N   LEU A  79     2958   2770   2946    -48   -145     -5       N  
ATOM    675  CA  LEU A  79       5.368  21.874  43.001  1.00 23.88           C  
ANISOU  675  CA  LEU A  79     3080   2891   3103    -51   -136     -2       C  
ATOM    676  C   LEU A  79       5.229  20.411  42.602  1.00 20.51           C  
ANISOU  676  C   LEU A  79     2670   2438   2684    -39   -103     20       C  
ATOM    677  O   LEU A  79       5.342  20.066  41.415  1.00 21.15           O  
ANISOU  677  O   LEU A  79     2754   2498   2786    -53    -84     15       O  
ATOM    678  CB  LEU A  79       6.807  22.158  43.459  1.00 21.85           C  
ANISOU  678  CB  LEU A  79     2794   2662   2848    -32   -160     -3       C  
ATOM    679  CG  LEU A  79       7.172  23.633  43.635  1.00 28.13           C  
ANISOU  679  CG  LEU A  79     3564   3476   3647    -50   -189    -32       C  
ATOM    680  CD1 LEU A  79       8.576  23.760  44.200  1.00 31.36           C  
ANISOU  680  CD1 LEU A  79     3940   3916   4059    -31   -213    -37       C  
ATOM    681  CD2 LEU A  79       7.065  24.384  42.312  1.00 29.39           C  
ANISOU  681  CD2 LEU A  79     3720   3611   3834    -80   -179    -46       C  
ATOM    682  N   ALA A  80       5.016  19.530  43.580  1.00 19.90           N  
ANISOU  682  N   ALA A  80     2606   2362   2592    -13    -91     43       N  
ATOM    683  CA  ALA A  80       4.846  18.113  43.270  1.00 20.09           C  
ANISOU  683  CA  ALA A  80     2649   2355   2631     -2    -52     64       C  
ATOM    684  C   ALA A  80       3.637  17.901  42.368  1.00 24.21           C  
ANISOU  684  C   ALA A  80     3187   2845   3167    -35    -29     47       C  
ATOM    685  O   ALA A  80       3.678  17.096  41.432  1.00 23.28           O  
ANISOU  685  O   ALA A  80     3074   2699   3071    -43     -2     44       O  
ATOM    686  CB  ALA A  80       4.707  17.308  44.563  1.00 24.32           C  
ANISOU  686  CB  ALA A  80     3197   2896   3147     33    -39     96       C  
ATOM    687  N   VAL A  81       2.542  18.603  42.648  1.00 21.80           N  
ANISOU  687  N   VAL A  81     2886   2545   2850    -53    -39     33       N  
ATOM    688  CA  VAL A  81       1.356  18.496  41.804  1.00 20.96           C  
ANISOU  688  CA  VAL A  81     2789   2417   2756    -84    -22     14       C  
ATOM    689  C   VAL A  81       1.639  19.032  40.405  1.00 17.42           C  
ANISOU  689  C   VAL A  81     2331   1969   2318   -105    -31     -9       C  
ATOM    690  O   VAL A  81       1.344  18.380  39.394  1.00 23.30           O  
ANISOU  690  O   VAL A  81     3082   2695   3079   -119    -10    -21       O  
ATOM    691  CB  VAL A  81       0.170  19.241  42.451  1.00 25.09           C  
ANISOU  691  CB  VAL A  81     3317   2952   3264    -95    -33      6       C  
ATOM    692  CG1 VAL A  81      -0.974  19.385  41.431  1.00 24.15           C  
ANISOU  692  CG1 VAL A  81     3199   2820   3157   -127    -25    -19       C  
ATOM    693  CG2 VAL A  81      -0.292  18.511  43.702  1.00 23.39           C  
ANISOU  693  CG2 VAL A  81     3117   2732   3040    -74    -13     30       C  
ATOM    694  N   ALA A  82       2.241  20.214  40.326  1.00 19.05           N  
ANISOU  694  N   ALA A  82     2522   2198   2519   -107    -59    -16       N  
ATOM    695  CA  ALA A  82       2.565  20.780  39.022  1.00 21.82           C  
ANISOU  695  CA  ALA A  82     2863   2548   2878   -123    -63    -31       C  
ATOM    696  C   ALA A  82       3.520  19.868  38.265  1.00 24.45           C  
ANISOU  696  C   ALA A  82     3196   2868   3226   -115    -44    -25       C  
ATOM    697  O   ALA A  82       3.372  19.686  37.060  1.00 20.88           O  
ANISOU  697  O   ALA A  82     2746   2407   2780   -128    -31    -38       O  
ATOM    698  CB  ALA A  82       3.181  22.170  39.177  1.00 22.84           C  
ANISOU  698  CB  ALA A  82     2975   2698   3005   -125    -90    -36       C  
ATOM    699  N   ASP A  83       4.494  19.275  38.965  1.00 19.74           N  
ANISOU  699  N   ASP A  83     2594   2272   2633    -90    -41     -6       N  
ATOM    700  CA  ASP A  83       5.409  18.336  38.309  1.00 23.65           C  
ANISOU  700  CA  ASP A  83     3088   2752   3146    -78    -19      2       C  
ATOM    701  C   ASP A  83       4.670  17.122  37.758  1.00 23.46           C  
ANISOU  701  C   ASP A  83     3085   2697   3133    -86     16     -4       C  
ATOM    702  O   ASP A  83       5.042  16.594  36.705  1.00 23.25           O  
ANISOU  702  O   ASP A  83     3059   2655   3118    -90     36    -14       O  
ATOM    703  CB  ASP A  83       6.497  17.853  39.279  1.00 20.18           C  
ANISOU  703  CB  ASP A  83     2639   2322   2708    -44    -21     28       C  
ATOM    704  CG  ASP A  83       7.434  18.938  39.729  1.00 19.37           C  
ANISOU  704  CG  ASP A  83     2509   2250   2600    -38    -55     27       C  
ATOM    705  OD1 ASP A  83       7.509  20.001  39.083  1.00 20.23           O  
ANISOU  705  OD1 ASP A  83     2606   2366   2713    -59    -69      9       O  
ATOM    706  OD2 ASP A  83       8.135  18.713  40.755  1.00 19.86           O  
ANISOU  706  OD2 ASP A  83     2560   2332   2655     -9    -67     44       O  
ATOM    707  N   LEU A  84       3.652  16.628  38.475  1.00 19.42           N  
ANISOU  707  N   LEU A  84     2587   2173   2618    -88     27     -1       N  
ATOM    708  CA  LEU A  84       2.897  15.485  37.961  1.00 21.71           C  
ANISOU  708  CA  LEU A  84     2893   2431   2926   -100     63    -12       C  
ATOM    709  C   LEU A  84       2.119  15.854  36.708  1.00 21.88           C  
ANISOU  709  C   LEU A  84     2913   2455   2945   -132     59    -48       C  
ATOM    710  O   LEU A  84       1.980  15.034  35.785  1.00 22.53           O  
ANISOU  710  O   LEU A  84     3003   2518   3042   -143     84    -69       O  
ATOM    711  CB  LEU A  84       1.959  14.929  39.042  1.00 22.66           C  
ANISOU  711  CB  LEU A  84     3026   2536   3047    -96     79      1       C  
ATOM    712  CG  LEU A  84       2.700  14.213  40.180  1.00 24.77           C  
ANISOU  712  CG  LEU A  84     3298   2797   3316    -57     94     41       C  
ATOM    713  CD1 LEU A  84       1.762  13.993  41.395  1.00 27.61           C  
ANISOU  713  CD1 LEU A  84     3670   3152   3668    -49    105     59       C  
ATOM    714  CD2 LEU A  84       3.252  12.876  39.708  1.00 25.05           C  
ANISOU  714  CD2 LEU A  84     3342   2795   3381    -45    135     49       C  
ATOM    715  N   PHE A  85       1.583  17.076  36.655  1.00 20.30           N  
ANISOU  715  N   PHE A  85     2706   2281   2726   -145     30    -58       N  
ATOM    716  CA  PHE A  85       0.967  17.534  35.413  1.00 24.12           C  
ANISOU  716  CA  PHE A  85     3186   2775   3202   -168     23    -87       C  
ATOM    717  C   PHE A  85       1.978  17.606  34.280  1.00 23.00           C  
ANISOU  717  C   PHE A  85     3040   2638   3060   -163     26    -92       C  
ATOM    718  O   PHE A  85       1.657  17.264  33.131  1.00 24.40           O  
ANISOU  718  O   PHE A  85     3221   2816   3236   -176     37   -117       O  
ATOM    719  CB  PHE A  85       0.310  18.902  35.615  1.00 23.42           C  
ANISOU  719  CB  PHE A  85     3090   2713   3095   -176     -7    -88       C  
ATOM    720  CG  PHE A  85      -1.077  18.814  36.184  1.00 27.08           C  
ANISOU  720  CG  PHE A  85     3557   3174   3557   -188     -6    -97       C  
ATOM    721  CD1 PHE A  85      -2.138  18.440  35.376  1.00 35.76           C  
ANISOU  721  CD1 PHE A  85     4655   4272   4658   -209      2   -125       C  
ATOM    722  CD2 PHE A  85      -1.316  19.083  37.516  1.00 33.96           C  
ANISOU  722  CD2 PHE A  85     4431   4047   4426   -179    -12    -79       C  
ATOM    723  CE1 PHE A  85      -3.422  18.345  35.893  1.00 43.21           C  
ANISOU  723  CE1 PHE A  85     5598   5214   5606   -222      5   -134       C  
ATOM    724  CE2 PHE A  85      -2.603  18.994  38.039  1.00 34.73           C  
ANISOU  724  CE2 PHE A  85     4531   4142   4524   -190     -7    -85       C  
ATOM    725  CZ  PHE A  85      -3.648  18.629  37.223  1.00 36.88           C  
ANISOU  725  CZ  PHE A  85     4800   4410   4803   -212      2   -112       C  
ATOM    726  N   MET A  86       3.194  18.085  34.566  1.00 19.79           N  
ANISOU  726  N   MET A  86     2624   2239   2656   -146     17    -70       N  
ATOM    727  CA  MET A  86       4.223  18.091  33.520  1.00 20.84           C  
ANISOU  727  CA  MET A  86     2752   2374   2793   -140     26    -72       C  
ATOM    728  C   MET A  86       4.476  16.689  33.009  1.00 20.71           C  
ANISOU  728  C   MET A  86     2746   2332   2791   -136     59    -81       C  
ATOM    729  O   MET A  86       4.535  16.458  31.796  1.00 22.45           O  
ANISOU  729  O   MET A  86     2971   2553   3008   -144     72   -102       O  
ATOM    730  CB  MET A  86       5.535  18.698  34.047  1.00 19.80           C  
ANISOU  730  CB  MET A  86     2602   2251   2668   -122     13    -49       C  
ATOM    731  CG  MET A  86       5.460  20.162  34.483  1.00 22.25           C  
ANISOU  731  CG  MET A  86     2900   2584   2971   -128    -16    -45       C  
ATOM    732  SD  MET A  86       7.115  20.708  35.098  1.00 27.41           S  
ANISOU  732  SD  MET A  86     3526   3247   3640   -110    -29    -27       S  
ATOM    733  CE  MET A  86       7.973  20.908  33.553  1.00 24.01           C  
ANISOU  733  CE  MET A  86     3089   2813   3220   -112     -9    -30       C  
ATOM    734  N   VAL A  87       4.610  15.729  33.924  1.00 20.97           N  
ANISOU  734  N   VAL A  87     2785   2342   2841   -123     76    -66       N  
ATOM    735  CA  VAL A  87       4.999  14.371  33.548  1.00 20.63           C  
ANISOU  735  CA  VAL A  87     2752   2267   2819   -116    113    -70       C  
ATOM    736  C   VAL A  87       3.913  13.707  32.710  1.00 22.67           C  
ANISOU  736  C   VAL A  87     3022   2510   3080   -141    133   -109       C  
ATOM    737  O   VAL A  87       4.177  13.180  31.626  1.00 23.27           O  
ANISOU  737  O   VAL A  87     3102   2578   3160   -146    153   -133       O  
ATOM    738  CB  VAL A  87       5.333  13.551  34.812  1.00 22.22           C  
ANISOU  738  CB  VAL A  87     2958   2448   3038    -91    129    -39       C  
ATOM    739  CG1 VAL A  87       5.379  12.062  34.512  1.00 23.02           C  
ANISOU  739  CG1 VAL A  87     3073   2507   3168    -86    176    -44       C  
ATOM    740  CG2 VAL A  87       6.691  14.024  35.387  1.00 21.41           C  
ANISOU  740  CG2 VAL A  87     2838   2366   2934    -61    111     -7       C  
ATOM    741  N   PHE A  88       2.669  13.742  33.181  1.00 20.88           N  
ANISOU  741  N   PHE A  88     2800   2283   2852   -158    127   -120       N  
ATOM    742  CA  PHE A  88       1.611  13.005  32.510  1.00 24.19           C  
ANISOU  742  CA  PHE A  88     3225   2687   3280   -184    146   -160       C  
ATOM    743  C   PHE A  88       0.943  13.805  31.401  1.00 24.53           C  
ANISOU  743  C   PHE A  88     3261   2765   3295   -205    122   -194       C  
ATOM    744  O   PHE A  88       0.539  13.219  30.389  1.00 28.19           O  
ANISOU  744  O   PHE A  88     3727   3226   3759   -221    136   -234       O  
ATOM    745  CB  PHE A  88       0.583  12.559  33.549  1.00 24.29           C  
ANISOU  745  CB  PHE A  88     3242   2679   3308   -193    157   -156       C  
ATOM    746  CG  PHE A  88       1.087  11.452  34.415  1.00 28.11           C  
ANISOU  746  CG  PHE A  88     3736   3122   3822   -172    194   -127       C  
ATOM    747  CD1 PHE A  88       1.397  10.230  33.859  1.00 37.39           C  
ANISOU  747  CD1 PHE A  88     4920   4259   5027   -173    236   -144       C  
ATOM    748  CD2 PHE A  88       1.317  11.651  35.755  1.00 36.53           C  
ANISOU  748  CD2 PHE A  88     4804   4190   4885   -148    188    -84       C  
ATOM    749  CE1 PHE A  88       1.892   9.205  34.637  1.00 45.99           C  
ANISOU  749  CE1 PHE A  88     6020   5307   6146   -149    275   -112       C  
ATOM    750  CE2 PHE A  88       1.812  10.640  36.541  1.00 43.65           C  
ANISOU  750  CE2 PHE A  88     5716   5058   5810   -122    223    -52       C  
ATOM    751  CZ  PHE A  88       2.099   9.410  35.980  1.00 45.18           C  
ANISOU  751  CZ  PHE A  88     5920   5210   6038   -122    268    -63       C  
ATOM    752  N   GLY A  89       0.837  15.114  31.567  1.00 25.90           N  
ANISOU  752  N   GLY A  89     3425   2972   3443   -202     87   -178       N  
ATOM    753  CA  GLY A  89       0.249  15.965  30.562  1.00 25.30           C  
ANISOU  753  CA  GLY A  89     3342   2931   3338   -214     65   -200       C  
ATOM    754  C   GLY A  89       1.158  16.305  29.407  1.00 31.81           C  
ANISOU  754  C   GLY A  89     4167   3773   4146   -203     66   -202       C  
ATOM    755  O   GLY A  89       0.714  16.296  28.251  1.00 25.39           O  
ANISOU  755  O   GLY A  89     3354   2982   3312   -212     64   -233       O  
ATOM    756  N   GLY A  90       2.420  16.633  29.692  1.00 20.90           N  
ANISOU  756  N   GLY A  90     2783   2386   2771   -184     67   -170       N  
ATOM    757  CA  GLY A  90       3.327  17.004  28.614  1.00 23.93           C  
ANISOU  757  CA  GLY A  90     3166   2785   3143   -173     73   -168       C  
ATOM    758  C   GLY A  90       4.380  15.963  28.246  1.00 25.13           C  
ANISOU  758  C   GLY A  90     3324   2913   3313   -161    105   -171       C  
ATOM    759  O   GLY A  90       4.577  15.702  27.061  1.00 23.40           O  
ANISOU  759  O   GLY A  90     3110   2702   3080   -161    119   -192       O  
ATOM    760  N   PHE A  91       5.058  15.345  29.225  1.00 22.46           N  
ANISOU  760  N   PHE A  91     2984   2547   3004   -149    117   -148       N  
ATOM    761  CA  PHE A  91       6.209  14.502  28.869  1.00 19.32           C  
ANISOU  761  CA  PHE A  91     2589   2127   2625   -132    148   -144       C  
ATOM    762  C   PHE A  91       5.796  13.232  28.157  1.00 20.43           C  
ANISOU  762  C   PHE A  91     2744   2244   2774   -143    180   -181       C  
ATOM    763  O   PHE A  91       6.585  12.689  27.382  1.00 20.24           O  
ANISOU  763  O   PHE A  91     2724   2210   2755   -133    206   -190       O  
ATOM    764  CB  PHE A  91       7.055  14.116  30.098  1.00 18.54           C  
ANISOU  764  CB  PHE A  91     2483   2007   2552   -111    153   -108       C  
ATOM    765  CG  PHE A  91       7.822  15.243  30.703  1.00 20.78           C  
ANISOU  765  CG  PHE A  91     2747   2314   2833    -98    126    -77       C  
ATOM    766  CD1 PHE A  91       7.714  16.545  30.209  1.00 22.87           C  
ANISOU  766  CD1 PHE A  91     3004   2608   3079   -108    103    -79       C  
ATOM    767  CD2 PHE A  91       8.665  15.011  31.778  1.00 22.33           C  
ANISOU  767  CD2 PHE A  91     2932   2504   3048    -75    124    -46       C  
ATOM    768  CE1 PHE A  91       8.439  17.592  30.770  1.00 24.29           C  
ANISOU  768  CE1 PHE A  91     3164   2803   3263   -100     81    -55       C  
ATOM    769  CE2 PHE A  91       9.397  16.055  32.346  1.00 23.28           C  
ANISOU  769  CE2 PHE A  91     3030   2647   3167    -66     97    -26       C  
ATOM    770  CZ  PHE A  91       9.270  17.345  31.860  1.00 27.32           C  
ANISOU  770  CZ  PHE A  91     3533   3181   3665    -81     76    -33       C  
ATOM    771  N   THR A  92       4.592  12.719  28.429  1.00 19.20           N  
ANISOU  771  N   THR A  92     2596   2078   2623   -163    181   -206       N  
ATOM    772  CA  THR A  92       4.125  11.551  27.680  1.00 19.74           C  
ANISOU  772  CA  THR A  92     2674   2124   2702   -178    212   -252       C  
ATOM    773  C   THR A  92       4.071  11.856  26.181  1.00 24.26           C  
ANISOU  773  C   THR A  92     3248   2729   3241   -185    208   -288       C  
ATOM    774  O   THR A  92       4.421  11.006  25.351  1.00 23.15           O  
ANISOU  774  O   THR A  92     3116   2574   3106   -185    238   -318       O  
ATOM    775  CB  THR A  92       2.758  11.097  28.219  1.00 26.25           C  
ANISOU  775  CB  THR A  92     3500   2933   3540   -203    213   -275       C  
ATOM    776  OG1 THR A  92       1.874  12.219  28.287  1.00 25.92           O  
ANISOU  776  OG1 THR A  92     3448   2931   3468   -215    173   -276       O  
ATOM    777  CG2 THR A  92       2.916  10.514  29.655  1.00 26.82           C  
ANISOU  777  CG2 THR A  92     3576   2967   3648   -190    230   -237       C  
ATOM    778  N   THR A  93       3.698  13.085  25.815  1.00 22.50           N  
ANISOU  778  N   THR A  93     3018   2551   2981   -187    173   -283       N  
ATOM    779  CA  THR A  93       3.753  13.464  24.398  1.00 19.33           C  
ANISOU  779  CA  THR A  93     2618   2186   2541   -185    170   -308       C  
ATOM    780  C   THR A  93       5.206  13.667  23.932  1.00 19.50           C  
ANISOU  780  C   THR A  93     2641   2206   2562   -160    188   -281       C  
ATOM    781  O   THR A  93       5.556  13.275  22.817  1.00 21.71           O  
ANISOU  781  O   THR A  93     2929   2495   2826   -155    208   -306       O  
ATOM    782  CB  THR A  93       2.896  14.732  24.154  1.00 28.28           C  
ANISOU  782  CB  THR A  93     3743   3368   3636   -189    132   -304       C  
ATOM    783  OG1 THR A  93       1.495  14.383  24.157  1.00 26.31           O  
ANISOU  783  OG1 THR A  93     3490   3127   3381   -213    119   -344       O  
ATOM    784  CG2 THR A  93       3.232  15.415  22.831  1.00 24.92           C  
ANISOU  784  CG2 THR A  93     3319   2982   3166   -175    129   -306       C  
ATOM    785  N   THR A  94       6.076  14.271  24.767  1.00 22.50           N  
ANISOU  785  N   THR A  94     3011   2577   2960   -144    182   -232       N  
ATOM    786  CA  THR A  94       7.479  14.401  24.344  1.00 19.53           C  
ANISOU  786  CA  THR A  94     2631   2198   2590   -122    201   -208       C  
ATOM    787  C   THR A  94       8.071  13.041  24.028  1.00 19.54           C  
ANISOU  787  C   THR A  94     2642   2166   2615   -116    242   -227       C  
ATOM    788  O   THR A  94       8.803  12.874  23.038  1.00 22.78           O  
ANISOU  788  O   THR A  94     3056   2581   3016   -104    265   -236       O  
ATOM    789  CB  THR A  94       8.362  15.031  25.423  1.00 19.32           C  
ANISOU  789  CB  THR A  94     2589   2164   2590   -108    190   -160       C  
ATOM    790  OG1 THR A  94       7.633  16.026  26.125  1.00 19.03           O  
ANISOU  790  OG1 THR A  94     2544   2144   2543   -118    155   -147       O  
ATOM    791  CG2 THR A  94       9.622  15.663  24.753  1.00 19.04           C  
ANISOU  791  CG2 THR A  94     2542   2139   2552    -90    203   -138       C  
ATOM    792  N   LEU A  95       7.749  12.053  24.849  1.00 20.51           N  
ANISOU  792  N   LEU A  95     2770   2253   2770   -122    254   -234       N  
ATOM    793  CA  LEU A  95       8.302  10.715  24.657  1.00 23.56           C  
ANISOU  793  CA  LEU A  95     3166   2600   3186   -114    297   -249       C  
ATOM    794  C   LEU A  95       7.792  10.097  23.362  1.00 22.01           C  
ANISOU  794  C   LEU A  95     2983   2408   2970   -129    317   -308       C  
ATOM    795  O   LEU A  95       8.570   9.591  22.544  1.00 24.22           O  
ANISOU  795  O   LEU A  95     3270   2680   3252   -116    348   -321       O  
ATOM    796  CB  LEU A  95       7.919   9.841  25.863  1.00 19.98           C  
ANISOU  796  CB  LEU A  95     2716   2104   2771   -116    309   -239       C  
ATOM    797  CG  LEU A  95       8.224   8.345  25.717  1.00 20.41           C  
ANISOU  797  CG  LEU A  95     2783   2108   2864   -111    360   -259       C  
ATOM    798  CD1 LEU A  95       9.739   8.097  25.471  1.00 22.91           C  
ANISOU  798  CD1 LEU A  95     3096   2414   3196    -78    386   -232       C  
ATOM    799  CD2 LEU A  95       7.721   7.586  26.985  1.00 24.15           C  
ANISOU  799  CD2 LEU A  95     3261   2541   3374   -111    373   -242       C  
ATOM    800  N   TYR A  96       6.472  10.142  23.164  1.00 20.78           N  
ANISOU  800  N   TYR A  96     2831   2269   2795   -155    298   -346       N  
ATOM    801  CA  TYR A  96       5.883   9.540  21.976  1.00 20.77           C  
ANISOU  801  CA  TYR A  96     2840   2280   2774   -172    311   -411       C  
ATOM    802  C   TYR A  96       6.408  10.208  20.716  1.00 24.01           C  
ANISOU  802  C   TYR A  96     3251   2735   3135   -156    307   -416       C  
ATOM    803  O   TYR A  96       6.725   9.535  19.722  1.00 24.85           O  
ANISOU  803  O   TYR A  96     3369   2841   3233   -154    336   -454       O  
ATOM    804  CB  TYR A  96       4.368   9.663  22.061  1.00 21.91           C  
ANISOU  804  CB  TYR A  96     2978   2444   2903   -201    283   -447       C  
ATOM    805  CG  TYR A  96       3.649   8.826  21.043  1.00 34.35           C  
ANISOU  805  CG  TYR A  96     4559   4026   4468   -223    297   -523       C  
ATOM    806  CD1 TYR A  96       3.561   7.444  21.188  1.00 33.97           C  
ANISOU  806  CD1 TYR A  96     4518   3923   4467   -239    338   -561       C  
ATOM    807  CD2 TYR A  96       3.058   9.414  19.940  1.00 40.63           C  
ANISOU  807  CD2 TYR A  96     5351   4882   5206   -228    270   -559       C  
ATOM    808  CE1 TYR A  96       2.901   6.673  20.236  1.00 36.31           C  
ANISOU  808  CE1 TYR A  96     4816   4225   4755   -263    351   -640       C  
ATOM    809  CE2 TYR A  96       2.387   8.655  18.995  1.00 43.87           C  
ANISOU  809  CE2 TYR A  96     5762   5306   5601   -248    278   -636       C  
ATOM    810  CZ  TYR A  96       2.303   7.293  19.148  1.00 49.81           C  
ANISOU  810  CZ  TYR A  96     6520   6003   6403   -268    318   -680       C  
ATOM    811  OH  TYR A  96       1.629   6.561  18.191  1.00 52.98           O  
ANISOU  811  OH  TYR A  96     6919   6419   6791   -292    326   -765       O  
ATOM    812  N   THR A  97       6.518  11.539  20.757  1.00 21.80           N  
ANISOU  812  N   THR A  97     2963   2494   2827   -145    276   -376       N  
ATOM    813  CA  THR A  97       7.033  12.311  19.633  1.00 21.42           C  
ANISOU  813  CA  THR A  97     2917   2487   2735   -127    276   -369       C  
ATOM    814  C   THR A  97       8.487  11.955  19.336  1.00 20.76           C  
ANISOU  814  C   THR A  97     2837   2381   2671   -104    314   -348       C  
ATOM    815  O   THR A  97       8.850  11.720  18.186  1.00 25.82           O  
ANISOU  815  O   THR A  97     3488   3039   3285    -93    337   -372       O  
ATOM    816  CB  THR A  97       6.897  13.807  19.956  1.00 21.17           C  
ANISOU  816  CB  THR A  97     2874   2487   2683   -120    241   -322       C  
ATOM    817  OG1 THR A  97       5.505  14.144  20.145  1.00 22.70           O  
ANISOU  817  OG1 THR A  97     3063   2705   2855   -139    207   -343       O  
ATOM    818  CG2 THR A  97       7.468  14.684  18.840  1.00 22.22           C  
ANISOU  818  CG2 THR A  97     3009   2660   2774    -98    247   -305       C  
ATOM    819  N  ASER A  98       9.335  11.916  20.374  0.78 20.54           N  
ANISOU  819  N  ASER A  98     2799   2318   2689    -93    322   -304       N  
ATOM    820  N  BSER A  98       9.333  11.904  20.369  0.22 20.55           N  
ANISOU  820  N  BSER A  98     2799   2318   2689    -93    322   -304       N  
ATOM    821  CA ASER A  98      10.746  11.582  20.166  0.78 22.97           C  
ANISOU  821  CA ASER A  98     3104   2605   3020    -69    357   -281       C  
ATOM    822  CA BSER A  98      10.740  11.577  20.144  0.22 22.89           C  
ANISOU  822  CA BSER A  98     3094   2595   3009    -69    358   -282       C  
ATOM    823  C  ASER A  98      10.919  10.154  19.652  0.78 21.16           C  
ANISOU  823  C  ASER A  98     2890   2343   2807    -69    400   -324       C  
ATOM    824  C  BSER A  98      10.917  10.148  19.643  0.22 21.16           C  
ANISOU  824  C  BSER A  98     2890   2343   2808    -69    400   -325       C  
ATOM    825  O  ASER A  98      11.877   9.869  18.930  0.78 23.76           O  
ANISOU  825  O  ASER A  98     3223   2668   3138    -50    434   -324       O  
ATOM    826  O  BSER A  98      11.874   9.863  18.915  0.22 23.76           O  
ANISOU  826  O  BSER A  98     3223   2668   3138    -50    434   -325       O  
ATOM    827  CB ASER A  98      11.522  11.773  21.476  0.78 20.88           C  
ANISOU  827  CB ASER A  98     2820   2314   2800    -57    351   -229       C  
ATOM    828  CB BSER A  98      11.534  11.784  21.429  0.22 20.90           C  
ANISOU  828  CB BSER A  98     2823   2317   2801    -57    352   -230       C  
ATOM    829  OG ASER A  98      11.367  13.086  22.004  0.78 20.07           O  
ANISOU  829  OG ASER A  98     2702   2237   2687    -60    314   -195       O  
ATOM    830  OG BSER A  98      11.007  10.980  22.466  0.22 20.39           O  
ANISOU  830  OG BSER A  98     2761   2219   2768    -67    350   -234       O  
ATOM    831  N   LEU A  99      10.020   9.238  20.035  1.00 21.26           N  
ANISOU  831  N   LEU A  99     2911   2330   2838    -90    403   -361       N  
ATOM    832  CA  LEU A  99      10.103   7.852  19.564  1.00 24.98           C  
ANISOU  832  CA  LEU A  99     3397   2763   3332    -93    447   -408       C  
ATOM    833  C   LEU A  99       9.916   7.780  18.055  1.00 27.34           C  
ANISOU  833  C   LEU A  99     3709   3098   3583    -96    458   -462       C  
ATOM    834  O   LEU A  99      10.573   6.993  17.366  1.00 23.40           O  
ANISOU  834  O   LEU A  99     3221   2579   3092    -85    500   -487       O  
ATOM    835  CB  LEU A  99       9.031   7.001  20.263  1.00 23.24           C  
ANISOU  835  CB  LEU A  99     3181   2507   3142   -120    449   -439       C  
ATOM    836  CG  LEU A  99       9.309   6.588  21.714  1.00 24.97           C  
ANISOU  836  CG  LEU A  99     3394   2679   3416   -111    457   -392       C  
ATOM    837  CD1 LEU A  99       8.090   5.936  22.378  1.00 30.44           C  
ANISOU  837  CD1 LEU A  99     4090   3342   4132   -139    457   -419       C  
ATOM    838  CD2 LEU A  99      10.465   5.641  21.752  1.00 26.11           C  
ANISOU  838  CD2 LEU A  99     3542   2776   3601    -85    507   -377       C  
ATOM    839  N   HIS A 100       8.979   8.565  17.542  1.00 22.88           N  
ANISOU  839  N   HIS A 100     3143   2586   2966   -110    421   -482       N  
ATOM    840  CA  HIS A 100       8.574   8.563  16.150  1.00 25.16           C  
ANISOU  840  CA  HIS A 100     3443   2920   3197   -112    422   -537       C  
ATOM    841  C   HIS A 100       9.334   9.571  15.303  1.00 30.51           C  
ANISOU  841  C   HIS A 100     4121   3643   3827    -83    421   -503       C  
ATOM    842  O   HIS A 100       9.291   9.490  14.073  1.00 32.37           O  
ANISOU  842  O   HIS A 100     4369   3917   4014    -75    432   -541       O  
ATOM    843  CB  HIS A 100       7.071   8.817  16.087  1.00 23.76           C  
ANISOU  843  CB  HIS A 100     3260   2778   2988   -139    380   -577       C  
ATOM    844  CG  HIS A 100       6.278   7.626  16.492  1.00 29.52           C  
ANISOU  844  CG  HIS A 100     3990   3466   3758   -170    393   -632       C  
ATOM    845  ND1 HIS A 100       6.035   6.571  15.633  1.00 32.99           N  
ANISOU  845  ND1 HIS A 100     4440   3900   4195   -184    420   -709       N  
ATOM    846  CD2 HIS A 100       5.751   7.274  17.686  1.00 28.22           C  
ANISOU  846  CD2 HIS A 100     3818   3260   3644   -190    388   -620       C  
ATOM    847  CE1 HIS A 100       5.360   5.634  16.276  1.00 36.07           C  
ANISOU  847  CE1 HIS A 100     4826   4242   4636   -214    433   -744       C  
ATOM    848  NE2 HIS A 100       5.171   6.038  17.519  1.00 31.61           N  
ANISOU  848  NE2 HIS A 100     4252   3655   4103   -216    415   -688       N  
ATOM    849  N   GLY A 101      10.051  10.494  15.918  1.00 24.74           N  
ANISOU  849  N   GLY A 101     3378   2910   3113    -66    412   -434       N  
ATOM    850  CA  GLY A 101      10.764  11.473  15.100  1.00 26.45           C  
ANISOU  850  CA  GLY A 101     3594   3164   3290    -40    418   -400       C  
ATOM    851  C   GLY A 101       9.943  12.660  14.630  1.00 24.51           C  
ANISOU  851  C   GLY A 101     3348   2979   2987    -39    381   -391       C  
ATOM    852  O   GLY A 101      10.449  13.465  13.837  1.00 26.89           O  
ANISOU  852  O   GLY A 101     3651   3313   3252    -15    392   -364       O  
ATOM    853  N   TYR A 102       8.704  12.804  15.098  1.00 26.27           N  
ANISOU  853  N   TYR A 102     3565   3214   3201    -62    342   -410       N  
ATOM    854  CA  TYR A 102       7.856  13.931  14.706  1.00 25.23           C  
ANISOU  854  CA  TYR A 102     3431   3139   3016    -58    306   -400       C  
ATOM    855  C   TYR A 102       6.572  13.904  15.525  1.00 25.53           C  
ANISOU  855  C   TYR A 102     3459   3176   3065    -86    267   -419       C  
ATOM    856  O   TYR A 102       6.253  12.918  16.197  1.00 26.37           O  
ANISOU  856  O   TYR A 102     3564   3243   3213   -109    271   -450       O  
ATOM    857  CB  TYR A 102       7.524  13.918  13.206  1.00 22.27           C  
ANISOU  857  CB  TYR A 102     3070   2823   2568    -42    311   -440       C  
ATOM    858  CG  TYR A 102       6.490  12.885  12.783  1.00 27.75           C  
ANISOU  858  CG  TYR A 102     3769   3533   3242    -65    301   -522       C  
ATOM    859  CD1 TYR A 102       6.812  11.527  12.727  1.00 27.57           C  
ANISOU  859  CD1 TYR A 102     3754   3469   3252    -79    333   -572       C  
ATOM    860  CD2 TYR A 102       5.200  13.281  12.409  1.00 25.87           C  
ANISOU  860  CD2 TYR A 102     3525   3352   2954    -72    260   -552       C  
ATOM    861  CE1 TYR A 102       5.860  10.568  12.323  1.00 27.89           C  
ANISOU  861  CE1 TYR A 102     3796   3520   3280   -104    327   -656       C  
ATOM    862  CE2 TYR A 102       4.253  12.348  11.996  1.00 28.47           C  
ANISOU  862  CE2 TYR A 102     3852   3698   3266    -95    249   -635       C  
ATOM    863  CZ  TYR A 102       4.586  10.993  11.956  1.00 33.57           C  
ANISOU  863  CZ  TYR A 102     4506   4299   3950   -113    283   -688       C  
ATOM    864  OH  TYR A 102       3.642  10.060  11.569  1.00 34.40           O  
ANISOU  864  OH  TYR A 102     4607   4417   4046   -141    275   -776       O  
ATOM    865  N   PHE A 103       5.833  15.011  15.462  1.00 22.24           N  
ANISOU  865  N   PHE A 103     3035   2801   2612    -81    232   -398       N  
ATOM    866  CA  PHE A 103       4.603  15.138  16.243  1.00 23.88           C  
ANISOU  866  CA  PHE A 103     3231   3011   2829   -105    195   -411       C  
ATOM    867  C   PHE A 103       3.495  14.342  15.554  1.00 25.33           C  
ANISOU  867  C   PHE A 103     3417   3228   2982   -122    183   -486       C  
ATOM    868  O   PHE A 103       2.687  14.876  14.795  1.00 26.12           O  
ANISOU  868  O   PHE A 103     3513   3388   3024   -114    157   -503       O  
ATOM    869  CB  PHE A 103       4.233  16.608  16.416  1.00 25.26           C  
ANISOU  869  CB  PHE A 103     3398   3219   2982    -92    166   -361       C  
ATOM    870  CG  PHE A 103       4.859  17.236  17.636  1.00 22.69           C  
ANISOU  870  CG  PHE A 103     3062   2850   2707    -93    165   -304       C  
ATOM    871  CD1 PHE A 103       4.285  17.073  18.865  1.00 23.36           C  
ANISOU  871  CD1 PHE A 103     3137   2906   2830   -116    146   -304       C  
ATOM    872  CD2 PHE A 103       6.073  17.942  17.538  1.00 23.04           C  
ANISOU  872  CD2 PHE A 103     3106   2885   2763    -72    187   -254       C  
ATOM    873  CE1 PHE A 103       4.825  17.661  20.015  1.00 24.89           C  
ANISOU  873  CE1 PHE A 103     3322   3068   3066   -115    142   -257       C  
ATOM    874  CE2 PHE A 103       6.642  18.495  18.668  1.00 24.58           C  
ANISOU  874  CE2 PHE A 103     3289   3045   3006    -75    184   -210       C  
ATOM    875  CZ  PHE A 103       6.026  18.348  19.922  1.00 27.58           C  
ANISOU  875  CZ  PHE A 103     3660   3402   3418    -96    159   -213       C  
ATOM    876  N   VAL A 104       3.452  13.042  15.856  1.00 25.21           N  
ANISOU  876  N   VAL A 104     3404   3170   3006   -146    202   -533       N  
ATOM    877  CA  VAL A 104       2.408  12.174  15.311  1.00 30.59           C  
ANISOU  877  CA  VAL A 104     4081   3870   3670   -170    194   -613       C  
ATOM    878  C   VAL A 104       1.033  12.719  15.659  1.00 36.39           C  
ANISOU  878  C   VAL A 104     4798   4640   4390   -186    149   -623       C  
ATOM    879  O   VAL A 104       0.102  12.665  14.846  1.00 35.79           O  
ANISOU  879  O   VAL A 104     4713   4619   4268   -192    126   -676       O  
ATOM    880  CB  VAL A 104       2.573  10.741  15.848  1.00 39.40           C  
ANISOU  880  CB  VAL A 104     5201   4919   4849   -196    228   -652       C  
ATOM    881  CG1 VAL A 104       1.558   9.803  15.184  1.00 41.42           C  
ANISOU  881  CG1 VAL A 104     5452   5194   5093   -224    225   -745       C  
ATOM    882  CG2 VAL A 104       3.977  10.261  15.614  1.00 35.87           C  
ANISOU  882  CG2 VAL A 104     4770   4436   4422   -176    273   -634       C  
ATOM    883  N   PHE A 105       0.891  13.260  16.868  1.00 28.71           N  
ANISOU  883  N   PHE A 105     3816   3637   3454   -192    136   -573       N  
ATOM    884  CA  PHE A 105      -0.383  13.779  17.371  1.00 28.85           C  
ANISOU  884  CA  PHE A 105     3815   3678   3468   -207     97   -576       C  
ATOM    885  C   PHE A 105      -0.740  15.127  16.780  1.00 33.42           C  
ANISOU  885  C   PHE A 105     4388   4323   3986   -181     65   -545       C  
ATOM    886  O   PHE A 105      -1.762  15.702  17.167  1.00 36.40           O  
ANISOU  886  O   PHE A 105     4749   4723   4357   -188     33   -541       O  
ATOM    887  CB  PHE A 105      -0.362  13.969  18.892  1.00 27.63           C  
ANISOU  887  CB  PHE A 105     3656   3472   3370   -218     96   -530       C  
ATOM    888  CG  PHE A 105      -0.100  12.731  19.696  1.00 50.21           C  
ANISOU  888  CG  PHE A 105     6520   6263   6293   -240    128   -547       C  
ATOM    889  CD1 PHE A 105      -0.468  11.476  19.242  1.00 51.89           C  
ANISOU  889  CD1 PHE A 105     6735   6462   6521   -263    148   -616       C  
ATOM    890  CD2 PHE A 105       0.501  12.847  20.958  1.00 44.45           C  
ANISOU  890  CD2 PHE A 105     5795   5486   5611   -236    138   -492       C  
ATOM    891  CE1 PHE A 105      -0.227  10.346  20.024  1.00 54.84           C  
ANISOU  891  CE1 PHE A 105     7114   6766   6958   -280    184   -625       C  
ATOM    892  CE2 PHE A 105       0.746  11.733  21.735  1.00 51.66           C  
ANISOU  892  CE2 PHE A 105     6712   6337   6578   -248    169   -499       C  
ATOM    893  CZ  PHE A 105       0.376  10.484  21.278  1.00 63.70           C  
ANISOU  893  CZ  PHE A 105     8240   7841   8121   -270    195   -562       C  
ATOM    894  N   GLY A 106       0.089  15.683  15.913  1.00 30.00           N  
ANISOU  894  N   GLY A 106     3968   3917   3513   -148     77   -518       N  
ATOM    895  CA  GLY A 106      -0.242  16.934  15.270  1.00 25.39           C  
ANISOU  895  CA  GLY A 106     3381   3395   2871   -118     54   -485       C  
ATOM    896  C   GLY A 106      -0.127  18.124  16.209  1.00 27.83           C  
ANISOU  896  C   GLY A 106     3685   3685   3206   -110     43   -413       C  
ATOM    897  O   GLY A 106       0.526  18.077  17.264  1.00 25.50           O  
ANISOU  897  O   GLY A 106     3392   3332   2967   -120     58   -382       O  
ATOM    898  N   PRO A 107      -0.722  19.243  15.802  1.00 26.27           N  
ANISOU  898  N   PRO A 107     3481   3538   2964    -86     20   -386       N  
ATOM    899  CA  PRO A 107      -0.656  20.451  16.633  1.00 24.13           C  
ANISOU  899  CA  PRO A 107     3205   3247   2716    -78     13   -321       C  
ATOM    900  C   PRO A 107      -1.247  20.246  18.001  1.00 24.26           C  
ANISOU  900  C   PRO A 107     3209   3223   2786   -109     -3   -326       C  
ATOM    901  O   PRO A 107      -0.836  20.919  18.944  1.00 25.08           O  
ANISOU  901  O   PRO A 107     3312   3291   2927   -109      0   -280       O  
ATOM    902  CB  PRO A 107      -1.456  21.484  15.820  1.00 32.46           C  
ANISOU  902  CB  PRO A 107     4254   4370   3710    -47    -10   -304       C  
ATOM    903  CG  PRO A 107      -1.302  21.022  14.392  1.00 25.10           C  
ANISOU  903  CG  PRO A 107     3331   3489   2715    -26     -1   -337       C  
ATOM    904  CD  PRO A 107      -1.244  19.516  14.446  1.00 30.48           C  
ANISOU  904  CD  PRO A 107     4014   4147   3419    -59      6   -406       C  
ATOM    905  N   THR A 108      -2.215  19.340  18.147  1.00 26.50           N  
ANISOU  905  N   THR A 108     3481   3512   3074   -136    -19   -383       N  
ATOM    906  CA  THR A 108      -2.726  19.083  19.483  1.00 26.96           C  
ANISOU  906  CA  THR A 108     3530   3528   3185   -164    -27   -384       C  
ATOM    907  C   THR A 108      -1.631  18.539  20.384  1.00 21.52           C  
ANISOU  907  C   THR A 108     2853   2774   2552   -174      2   -365       C  
ATOM    908  O   THR A 108      -1.519  18.939  21.549  1.00 24.37           O  
ANISOU  908  O   THR A 108     3210   3099   2948   -180     -1   -330       O  
ATOM    909  CB  THR A 108      -3.894  18.109  19.418  1.00 29.59           C  
ANISOU  909  CB  THR A 108     3847   3874   3520   -193    -41   -452       C  
ATOM    910  OG1 THR A 108      -4.947  18.730  18.679  1.00 35.44           O  
ANISOU  910  OG1 THR A 108     4572   4684   4210   -180    -73   -466       O  
ATOM    911  CG2 THR A 108      -4.366  17.779  20.841  1.00 33.58           C  
ANISOU  911  CG2 THR A 108     4345   4331   4084   -221    -41   -448       C  
ATOM    912  N   GLY A 109      -0.805  17.629  19.856  1.00 22.08           N  
ANISOU  912  N   GLY A 109     2936   2828   2627   -175     29   -387       N  
ATOM    913  CA  GLY A 109       0.338  17.173  20.631  1.00 26.94           C  
ANISOU  913  CA  GLY A 109     3561   3386   3291   -177     57   -362       C  
ATOM    914  C   GLY A 109       1.282  18.308  20.974  1.00 20.43           C  
ANISOU  914  C   GLY A 109     2738   2553   2473   -155     60   -298       C  
ATOM    915  O   GLY A 109       1.780  18.400  22.093  1.00 21.64           O  
ANISOU  915  O   GLY A 109     2888   2668   2668   -159     63   -269       O  
ATOM    916  N   CYS A 110       1.541  19.185  20.009  1.00 21.91           N  
ANISOU  916  N   CYS A 110     2928   2778   2620   -131     60   -278       N  
ATOM    917  CA  CYS A 110       2.453  20.297  20.248  1.00 21.16           C  
ANISOU  917  CA  CYS A 110     2832   2673   2536   -112     68   -221       C  
ATOM    918  C   CYS A 110       1.925  21.208  21.350  1.00 23.14           C  
ANISOU  918  C   CYS A 110     3072   2913   2809   -119     44   -192       C  
ATOM    919  O   CYS A 110       2.685  21.662  22.207  1.00 20.12           O  
ANISOU  919  O   CYS A 110     2684   2498   2463   -119     50   -159       O  
ATOM    920  CB  CYS A 110       2.652  21.055  18.935  1.00 24.05           C  
ANISOU  920  CB  CYS A 110     3205   3082   2853    -83     76   -204       C  
ATOM    921  SG  CYS A 110       3.687  22.507  19.006  1.00 22.05           S  
ANISOU  921  SG  CYS A 110     2948   2816   2614    -60     94   -135       S  
ATOM    922  N   ASN A 111       0.609  21.461  21.349  1.00 23.22           N  
ANISOU  922  N   ASN A 111     3075   2952   2796   -125     18   -208       N  
ATOM    923  CA  ASN A 111      -0.027  22.256  22.394  1.00 22.52           C  
ANISOU  923  CA  ASN A 111     2976   2853   2726   -132     -3   -186       C  
ATOM    924  C   ASN A 111       0.119  21.610  23.764  1.00 22.00           C  
ANISOU  924  C   ASN A 111     2908   2742   2709   -154     -3   -191       C  
ATOM    925  O   ASN A 111       0.413  22.301  24.743  1.00 22.52           O  
ANISOU  925  O   ASN A 111     2969   2786   2801   -154     -8   -160       O  
ATOM    926  CB  ASN A 111      -1.515  22.445  22.080  1.00 24.97           C  
ANISOU  926  CB  ASN A 111     3277   3205   3005   -134    -30   -209       C  
ATOM    927  CG  ASN A 111      -1.759  23.511  21.049  1.00 27.04           C  
ANISOU  927  CG  ASN A 111     3540   3515   3222   -105    -36   -186       C  
ATOM    928  OD1 ASN A 111      -0.872  24.307  20.745  1.00 26.94           O  
ANISOU  928  OD1 ASN A 111     3534   3496   3208    -84    -17   -145       O  
ATOM    929  ND2 ASN A 111      -2.986  23.545  20.499  1.00 30.35           N  
ANISOU  929  ND2 ASN A 111     3948   3981   3602   -101    -59   -211       N  
ATOM    930  N   LEU A 112      -0.108  20.292  23.860  1.00 19.86           N  
ANISOU  930  N   LEU A 112     2639   2456   2449   -171      4   -229       N  
ATOM    931  CA  LEU A 112       0.045  19.604  25.150  1.00 22.25           C  
ANISOU  931  CA  LEU A 112     2943   2716   2796   -186     10   -228       C  
ATOM    932  C   LEU A 112       1.461  19.767  25.680  1.00 23.31           C  
ANISOU  932  C   LEU A 112     3080   2821   2957   -174     25   -193       C  
ATOM    933  O   LEU A 112       1.683  20.103  26.854  1.00 22.47           O  
ANISOU  933  O   LEU A 112     2969   2695   2876   -175     18   -169       O  
ATOM    934  CB  LEU A 112      -0.239  18.104  24.971  1.00 21.54           C  
ANISOU  934  CB  LEU A 112     2858   2609   2718   -203     27   -273       C  
ATOM    935  CG  LEU A 112      -1.683  17.761  24.629  1.00 32.79           C  
ANISOU  935  CG  LEU A 112     4274   4058   4127   -222     12   -317       C  
ATOM    936  CD1 LEU A 112      -1.763  16.295  24.241  1.00 29.80           C  
ANISOU  936  CD1 LEU A 112     3900   3660   3764   -239     35   -366       C  
ATOM    937  CD2 LEU A 112      -2.529  18.065  25.836  1.00 33.21           C  
ANISOU  937  CD2 LEU A 112     4318   4098   4200   -233     -3   -304       C  
ATOM    938  N   GLU A 113       2.427  19.467  24.820  1.00 22.70           N  
ANISOU  938  N   GLU A 113     3009   2744   2874   -162     47   -193       N  
ATOM    939  CA  GLU A 113       3.827  19.455  25.225  1.00 20.64           C  
ANISOU  939  CA  GLU A 113     2746   2457   2641   -151     64   -165       C  
ATOM    940  C   GLU A 113       4.249  20.841  25.696  1.00 22.22           C  
ANISOU  940  C   GLU A 113     2934   2660   2848   -143     51   -126       C  
ATOM    941  O   GLU A 113       4.843  20.996  26.777  1.00 20.56           O  
ANISOU  941  O   GLU A 113     2715   2429   2668   -143     47   -107       O  
ATOM    942  CB  GLU A 113       4.666  18.974  24.031  1.00 20.28           C  
ANISOU  942  CB  GLU A 113     2707   2415   2583   -139     91   -174       C  
ATOM    943  CG  GLU A 113       5.979  18.197  24.353  1.00 20.32           C  
ANISOU  943  CG  GLU A 113     2711   2387   2623   -130    117   -163       C  
ATOM    944  CD  GLU A 113       7.130  19.084  24.861  1.00 21.86           C  
ANISOU  944  CD  GLU A 113     2891   2573   2841   -118    117   -122       C  
ATOM    945  OE1 GLU A 113       7.243  20.257  24.452  1.00 19.67           O  
ANISOU  945  OE1 GLU A 113     2607   2314   2550   -112    112   -102       O  
ATOM    946  OE2 GLU A 113       7.946  18.575  25.669  1.00 21.65           O  
ANISOU  946  OE2 GLU A 113     2857   2522   2848   -113    125   -109       O  
ATOM    947  N   GLY A 114       3.951  21.866  24.884  1.00 22.55           N  
ANISOU  947  N   GLY A 114     2975   2730   2862   -134     46   -116       N  
ATOM    948  CA  GLY A 114       4.357  23.220  25.233  1.00 20.74           C  
ANISOU  948  CA  GLY A 114     2735   2498   2646   -128     41    -81       C  
ATOM    949  C   GLY A 114       3.602  23.760  26.432  1.00 21.67           C  
ANISOU  949  C   GLY A 114     2846   2610   2776   -139     16    -77       C  
ATOM    950  O   GLY A 114       4.187  24.382  27.325  1.00 20.91           O  
ANISOU  950  O   GLY A 114     2739   2496   2708   -140     12    -59       O  
ATOM    951  N   PHE A 115       2.292  23.524  26.478  1.00 20.47           N  
ANISOU  951  N   PHE A 115     2700   2474   2606   -148      0    -97       N  
ATOM    952  CA  PHE A 115       1.486  24.109  27.554  1.00 20.02           C  
ANISOU  952  CA  PHE A 115     2636   2413   2558   -156    -21    -92       C  
ATOM    953  C   PHE A 115       1.908  23.565  28.913  1.00 21.43           C  
ANISOU  953  C   PHE A 115     2812   2563   2767   -164    -24    -92       C  
ATOM    954  O   PHE A 115       2.088  24.329  29.878  1.00 20.95           O  
ANISOU  954  O   PHE A 115     2743   2493   2723   -165    -35    -76       O  
ATOM    955  CB  PHE A 115      -0.006  23.833  27.326  1.00 22.60           C  
ANISOU  955  CB  PHE A 115     2964   2761   2860   -164    -36   -116       C  
ATOM    956  CG  PHE A 115      -0.873  24.226  28.496  1.00 23.06           C  
ANISOU  956  CG  PHE A 115     3017   2813   2931   -174    -54   -114       C  
ATOM    957  CD1 PHE A 115      -1.270  25.537  28.668  1.00 21.18           C  
ANISOU  957  CD1 PHE A 115     2773   2584   2690   -166    -64    -94       C  
ATOM    958  CD2 PHE A 115      -1.292  23.269  29.427  1.00 23.48           C  
ANISOU  958  CD2 PHE A 115     3073   2849   3000   -188    -55   -131       C  
ATOM    959  CE1 PHE A 115      -2.090  25.902  29.766  1.00 21.59           C  
ANISOU  959  CE1 PHE A 115     2821   2630   2753   -174    -78    -94       C  
ATOM    960  CE2 PHE A 115      -2.100  23.622  30.518  1.00 26.31           C  
ANISOU  960  CE2 PHE A 115     3426   3202   3367   -195    -68   -128       C  
ATOM    961  CZ  PHE A 115      -2.485  24.950  30.683  1.00 24.27           C  
ANISOU  961  CZ  PHE A 115     3162   2955   3104   -188    -81   -111       C  
ATOM    962  N   PHE A 116       2.071  22.239  29.026  1.00 17.42           N  
ANISOU  962  N   PHE A 116     2311   2042   2267   -169    -14   -108       N  
ATOM    963  CA  PHE A 116       2.339  21.735  30.369  1.00 19.82           C  
ANISOU  963  CA  PHE A 116     2613   2323   2595   -171    -16   -102       C  
ATOM    964  C   PHE A 116       3.756  22.048  30.830  1.00 23.58           C  
ANISOU  964  C   PHE A 116     3079   2788   3091   -160    -13    -80       C  
ATOM    965  O   PHE A 116       3.985  22.209  32.034  1.00 21.17           O  
ANISOU  965  O   PHE A 116     2767   2476   2800   -158    -24    -70       O  
ATOM    966  CB  PHE A 116       2.050  20.244  30.434  1.00 23.47           C  
ANISOU  966  CB  PHE A 116     3085   2769   3064   -177      0   -122       C  
ATOM    967  CG  PHE A 116       0.588  19.961  30.619  1.00 25.54           C  
ANISOU  967  CG  PHE A 116     3350   3036   3318   -193     -7   -143       C  
ATOM    968  CD1 PHE A 116      -0.030  20.238  31.838  1.00 25.27           C  
ANISOU  968  CD1 PHE A 116     3314   2996   3291   -197    -20   -134       C  
ATOM    969  CD2 PHE A 116      -0.174  19.486  29.571  1.00 23.26           C  
ANISOU  969  CD2 PHE A 116     3064   2760   3014   -203     -3   -175       C  
ATOM    970  CE1 PHE A 116      -1.381  20.012  32.007  1.00 26.09           C  
ANISOU  970  CE1 PHE A 116     3417   3104   3391   -211    -24   -153       C  
ATOM    971  CE2 PHE A 116      -1.535  19.252  29.725  1.00 27.53           C  
ANISOU  971  CE2 PHE A 116     3601   3307   3550   -219    -10   -198       C  
ATOM    972  CZ  PHE A 116      -2.142  19.518  30.950  1.00 27.21           C  
ANISOU  972  CZ  PHE A 116     3558   3258   3522   -224    -19   -185       C  
ATOM    973  N   ALA A 117       4.715  22.133  29.904  1.00 19.80           N  
ANISOU  973  N   ALA A 117     2597   2310   2615   -151      3    -74       N  
ATOM    974  CA  ALA A 117       6.061  22.536  30.317  1.00 20.30           C  
ANISOU  974  CA  ALA A 117     2644   2366   2702   -142      5    -55       C  
ATOM    975  C   ALA A 117       6.091  24.002  30.743  1.00 19.81           C  
ANISOU  975  C   ALA A 117     2568   2310   2647   -146    -10    -44       C  
ATOM    976  O   ALA A 117       6.727  24.358  31.741  1.00 22.40           O  
ANISOU  976  O   ALA A 117     2881   2633   2996   -145    -22    -37       O  
ATOM    977  CB  ALA A 117       7.052  22.285  29.171  1.00 19.84           C  
ANISOU  977  CB  ALA A 117     2585   2307   2648   -133     31    -52       C  
ATOM    978  N   THR A 118       5.417  24.872  29.981  1.00 19.90           N  
ANISOU  978  N   THR A 118     2585   2333   2643   -149    -10    -42       N  
ATOM    979  CA  THR A 118       5.355  26.289  30.345  1.00 18.38           C  
ANISOU  979  CA  THR A 118     2381   2140   2462   -152    -19    -31       C  
ATOM    980  C   THR A 118       4.646  26.482  31.675  1.00 20.76           C  
ANISOU  980  C   THR A 118     2681   2440   2766   -160    -43    -38       C  
ATOM    981  O   THR A 118       5.111  27.234  32.539  1.00 19.90           O  
ANISOU  981  O   THR A 118     2558   2324   2677   -163    -53    -36       O  
ATOM    982  CB  THR A 118       4.625  27.069  29.249  1.00 22.10           C  
ANISOU  982  CB  THR A 118     2861   2624   2912   -148    -11    -23       C  
ATOM    983  OG1 THR A 118       5.290  26.836  28.007  1.00 20.36           O  
ANISOU  983  OG1 THR A 118     2643   2409   2684   -137     13    -15       O  
ATOM    984  CG2 THR A 118       4.613  28.566  29.569  1.00 20.68           C  
ANISOU  984  CG2 THR A 118     2670   2437   2751   -149    -12     -8       C  
ATOM    985  N   LEU A 119       3.530  25.782  31.862  1.00 22.02           N  
ANISOU  985  N   LEU A 119     2855   2606   2906   -164    -51    -50       N  
ATOM    986  CA  LEU A 119       2.779  25.884  33.107  1.00 22.97           C  
ANISOU  986  CA  LEU A 119     2977   2726   3026   -170    -69    -56       C  
ATOM    987  C   LEU A 119       3.626  25.428  34.292  1.00 22.58           C  
ANISOU  987  C   LEU A 119     2919   2668   2991   -165    -76    -54       C  
ATOM    988  O   LEU A 119       3.747  26.133  35.298  1.00 21.77           O  
ANISOU  988  O   LEU A 119     2807   2568   2897   -166    -91    -55       O  
ATOM    989  CB  LEU A 119       1.501  25.052  32.980  1.00 22.02           C  
ANISOU  989  CB  LEU A 119     2870   2611   2887   -175    -70    -69       C  
ATOM    990  CG  LEU A 119       0.657  25.023  34.260  1.00 31.25           C  
ANISOU  990  CG  LEU A 119     4041   3778   4055   -180    -83    -74       C  
ATOM    991  CD1 LEU A 119      -0.089  26.360  34.350  1.00 26.93           C  
ANISOU  991  CD1 LEU A 119     3490   3240   3504   -182    -94    -71       C  
ATOM    992  CD2 LEU A 119      -0.309  23.830  34.207  1.00 29.12           C  
ANISOU  992  CD2 LEU A 119     3782   3506   3777   -186    -75    -87       C  
ATOM    993  N   GLY A 120       4.290  24.279  34.154  1.00 20.33           N  
ANISOU  993  N   GLY A 120     2637   2378   2711   -158    -64    -53       N  
ATOM    994  CA  GLY A 120       5.098  23.773  35.246  1.00 21.21           C  
ANISOU  994  CA  GLY A 120     2740   2487   2832   -147    -71    -47       C  
ATOM    995  C   GLY A 120       6.269  24.681  35.576  1.00 22.64           C  
ANISOU  995  C   GLY A 120     2896   2673   3032   -144    -81    -43       C  
ATOM    996  O   GLY A 120       6.571  24.920  36.749  1.00 21.36           O  
ANISOU  996  O   GLY A 120     2723   2520   2873   -139   -100    -45       O  
ATOM    997  N   GLY A 121       6.959  25.177  34.555  1.00 21.51           N  
ANISOU  997  N   GLY A 121     2744   2527   2904   -147    -68    -40       N  
ATOM    998  CA  GLY A 121       8.071  26.086  34.814  1.00 22.66           C  
ANISOU  998  CA  GLY A 121     2862   2674   3075   -148    -74    -40       C  
ATOM    999  C   GLY A 121       7.624  27.384  35.474  1.00 24.95           C  
ANISOU  999  C   GLY A 121     3144   2965   3370   -160    -90    -50       C  
ATOM   1000  O   GLY A 121       8.284  27.896  36.386  1.00 20.85           O  
ANISOU 1000  O   GLY A 121     2603   2452   2867   -162   -107    -60       O  
ATOM   1001  N   GLU A 122       6.488  27.936  35.028  1.00 19.28           N  
ANISOU 1001  N   GLU A 122     2443   2244   2640   -168    -86    -49       N  
ATOM   1002  CA  GLU A 122       6.026  29.198  35.614  1.00 18.88           C  
ANISOU 1002  CA  GLU A 122     2386   2191   2598   -177    -97    -58       C  
ATOM   1003  C   GLU A 122       5.428  29.000  37.005  1.00 21.40           C  
ANISOU 1003  C   GLU A 122     2710   2521   2901   -176   -121    -71       C  
ATOM   1004  O   GLU A 122       5.541  29.896  37.851  1.00 21.83           O  
ANISOU 1004  O   GLU A 122     2752   2577   2967   -183   -134    -85       O  
ATOM   1005  CB  GLU A 122       5.020  29.888  34.680  1.00 18.86           C  
ANISOU 1005  CB  GLU A 122     2398   2182   2586   -180    -83    -49       C  
ATOM   1006  CG  GLU A 122       5.725  30.523  33.473  1.00 17.54           C  
ANISOU 1006  CG  GLU A 122     2223   2004   2438   -179    -58    -34       C  
ATOM   1007  CD  GLU A 122       6.530  31.750  33.860  1.00 22.67           C  
ANISOU 1007  CD  GLU A 122     2849   2638   3128   -189    -53    -40       C  
ATOM   1008  OE1 GLU A 122       6.181  32.359  34.867  1.00 24.74           O  
ANISOU 1008  OE1 GLU A 122     3105   2898   3397   -197    -69    -56       O  
ATOM   1009  OE2 GLU A 122       7.513  32.117  33.150  1.00 21.71           O  
ANISOU 1009  OE2 GLU A 122     2712   2504   3032   -190    -31    -30       O  
ATOM   1010  N   ILE A 123       4.818  27.848  37.280  1.00 20.36           N  
ANISOU 1010  N   ILE A 123     2596   2395   2745   -168   -123    -67       N  
ATOM   1011  CA  ILE A 123       4.441  27.578  38.672  1.00 20.43           C  
ANISOU 1011  CA  ILE A 123     2609   2416   2739   -163   -141    -74       C  
ATOM   1012  C   ILE A 123       5.682  27.586  39.557  1.00 23.37           C  
ANISOU 1012  C   ILE A 123     2958   2801   3120   -154   -157    -80       C  
ATOM   1013  O   ILE A 123       5.664  28.133  40.663  1.00 21.18           O  
ANISOU 1013  O   ILE A 123     2672   2536   2837   -153   -177    -95       O  
ATOM   1014  CB  ILE A 123       3.661  26.263  38.798  1.00 20.24           C  
ANISOU 1014  CB  ILE A 123     2606   2391   2694   -155   -134    -65       C  
ATOM   1015  CG1 ILE A 123       2.245  26.494  38.248  1.00 23.22           C  
ANISOU 1015  CG1 ILE A 123     2999   2764   3061   -166   -126    -68       C  
ATOM   1016  CG2 ILE A 123       3.559  25.826  40.285  1.00 23.56           C  
ANISOU 1016  CG2 ILE A 123     3029   2824   3098   -142   -147    -65       C  
ATOM   1017  CD1 ILE A 123       1.452  25.227  37.994  1.00 24.67           C  
ANISOU 1017  CD1 ILE A 123     3199   2942   3232   -165   -113    -64       C  
ATOM   1018  N   ALA A 124       6.791  27.016  39.072  1.00 18.99           N  
ANISOU 1018  N   ALA A 124     2390   2245   2579   -147   -150    -72       N  
ATOM   1019  CA  ALA A 124       8.013  27.021  39.875  1.00 23.79           C  
ANISOU 1019  CA  ALA A 124     2972   2872   3197   -136   -168    -79       C  
ATOM   1020  C   ALA A 124       8.535  28.440  40.081  1.00 21.24           C  
ANISOU 1020  C   ALA A 124     2622   2550   2899   -153   -179   -102       C  
ATOM   1021  O   ALA A 124       8.909  28.816  41.199  1.00 23.54           O  
ANISOU 1021  O   ALA A 124     2894   2862   3187   -150   -204   -122       O  
ATOM   1022  CB  ALA A 124       9.078  26.134  39.216  1.00 21.87           C  
ANISOU 1022  CB  ALA A 124     2718   2625   2967   -124   -154    -64       C  
ATOM   1023  N   LEU A 125       8.579  29.247  39.022  1.00 19.03           N  
ANISOU 1023  N   LEU A 125     2338   2248   2645   -169   -160   -101       N  
ATOM   1024  CA  LEU A 125       9.128  30.602  39.176  1.00 19.44           C  
ANISOU 1024  CA  LEU A 125     2362   2293   2730   -187   -163   -123       C  
ATOM   1025  C   LEU A 125       8.276  31.426  40.136  1.00 21.51           C  
ANISOU 1025  C   LEU A 125     2631   2559   2983   -195   -179   -145       C  
ATOM   1026  O   LEU A 125       8.792  32.073  41.051  1.00 24.35           O  
ANISOU 1026  O   LEU A 125     2966   2930   3355   -202   -199   -174       O  
ATOM   1027  CB  LEU A 125       9.222  31.291  37.803  1.00 19.35           C  
ANISOU 1027  CB  LEU A 125     2352   2254   2748   -199   -131   -110       C  
ATOM   1028  CG  LEU A 125       9.686  32.754  37.780  1.00 23.29           C  
ANISOU 1028  CG  LEU A 125     2825   2734   3290   -218   -122   -128       C  
ATOM   1029  CD1 LEU A 125      11.076  32.975  38.525  1.00 19.22           C  
ANISOU 1029  CD1 LEU A 125     2265   2230   2806   -226   -139   -156       C  
ATOM   1030  CD2 LEU A 125       9.765  33.249  36.325  1.00 24.55           C  
ANISOU 1030  CD2 LEU A 125     2990   2866   3473   -222    -82   -104       C  
ATOM   1031  N   TRP A 126       6.953  31.389  39.969  1.00 23.57           N  
ANISOU 1031  N   TRP A 126     2923   2812   3221   -194   -172   -134       N  
ATOM   1032  CA  TRP A 126       6.117  32.190  40.865  1.00 24.48           C  
ANISOU 1032  CA  TRP A 126     3044   2929   3328   -200   -184   -154       C  
ATOM   1033  C   TRP A 126       6.083  31.606  42.278  1.00 25.98           C  
ANISOU 1033  C   TRP A 126     3234   3149   3486   -187   -211   -167       C  
ATOM   1034  O   TRP A 126       5.901  32.353  43.254  1.00 22.93           O  
ANISOU 1034  O   TRP A 126     2842   2772   3097   -191   -227   -194       O  
ATOM   1035  CB  TRP A 126       4.715  32.345  40.260  1.00 20.17           C  
ANISOU 1035  CB  TRP A 126     2527   2369   2769   -201   -167   -137       C  
ATOM   1036  CG  TRP A 126       4.700  33.322  39.098  1.00 21.56           C  
ANISOU 1036  CG  TRP A 126     2699   2517   2974   -211   -142   -127       C  
ATOM   1037  CD1 TRP A 126       4.610  33.020  37.749  1.00 23.84           C  
ANISOU 1037  CD1 TRP A 126     2997   2798   3262   -207   -120   -101       C  
ATOM   1038  CD2 TRP A 126       4.805  34.750  39.179  1.00 24.39           C  
ANISOU 1038  CD2 TRP A 126     3045   2856   3368   -225   -132   -143       C  
ATOM   1039  NE1 TRP A 126       4.642  34.176  37.001  1.00 22.34           N  
ANISOU 1039  NE1 TRP A 126     2802   2585   3100   -213    -97    -94       N  
ATOM   1040  CE2 TRP A 126       4.745  35.252  37.854  1.00 21.78           C  
ANISOU 1040  CE2 TRP A 126     2717   2502   3055   -225   -102   -118       C  
ATOM   1041  CE3 TRP A 126       4.908  35.656  40.248  1.00 26.58           C  
ANISOU 1041  CE3 TRP A 126     3308   3130   3661   -236   -144   -176       C  
ATOM   1042  CZ2 TRP A 126       4.810  36.615  37.566  1.00 21.86           C  
ANISOU 1042  CZ2 TRP A 126     2718   2484   3105   -234    -79   -120       C  
ATOM   1043  CZ3 TRP A 126       4.988  37.014  39.960  1.00 28.73           C  
ANISOU 1043  CZ3 TRP A 126     3569   3371   3976   -250   -122   -185       C  
ATOM   1044  CH2 TRP A 126       4.935  37.481  38.625  1.00 21.65           C  
ANISOU 1044  CH2 TRP A 126     2678   2448   3102   -248    -88   -154       C  
ATOM   1045  N   SER A 127       6.301  30.289  42.424  1.00 20.82           N  
ANISOU 1045  N   SER A 127     2589   2512   2809   -168   -215   -148       N  
ATOM   1046  CA  SER A 127       6.511  29.731  43.757  1.00 24.37           C  
ANISOU 1046  CA  SER A 127     3036   2994   3229   -148   -239   -155       C  
ATOM   1047  C   SER A 127       7.739  30.328  44.417  1.00 24.15           C  
ANISOU 1047  C   SER A 127     2971   2989   3216   -150   -264   -185       C  
ATOM   1048  O   SER A 127       7.733  30.576  45.627  1.00 22.16           O  
ANISOU 1048  O   SER A 127     2713   2766   2942   -142   -288   -208       O  
ATOM   1049  CB  SER A 127       6.634  28.205  43.705  1.00 23.18           C  
ANISOU 1049  CB  SER A 127     2898   2851   3058   -125   -233   -124       C  
ATOM   1050  OG  SER A 127       5.404  27.630  43.289  1.00 24.83           O  
ANISOU 1050  OG  SER A 127     3140   3042   3253   -125   -212   -105       O  
ATOM   1051  N   LEU A 128       8.815  30.545  43.655  1.00 21.28           N  
ANISOU 1051  N   LEU A 128     2580   2615   2889   -159   -257   -187       N  
ATOM   1052  CA  LEU A 128       9.993  31.156  44.257  1.00 20.91           C  
ANISOU 1052  CA  LEU A 128     2491   2590   2862   -165   -280   -221       C  
ATOM   1053  C   LEU A 128       9.720  32.595  44.679  1.00 24.17           C  
ANISOU 1053  C   LEU A 128     2893   2994   3295   -190   -286   -262       C  
ATOM   1054  O   LEU A 128      10.327  33.087  45.632  1.00 26.93           O  
ANISOU 1054  O   LEU A 128     3214   3371   3646   -192   -314   -301       O  
ATOM   1055  CB  LEU A 128      11.173  31.120  43.279  1.00 23.85           C  
ANISOU 1055  CB  LEU A 128     2835   2950   3276   -172   -266   -214       C  
ATOM   1056  CG  LEU A 128      11.601  29.727  42.812  1.00 25.07           C  
ANISOU 1056  CG  LEU A 128     2996   3110   3418   -148   -258   -178       C  
ATOM   1057  CD1 LEU A 128      12.811  29.869  41.878  1.00 24.04           C  
ANISOU 1057  CD1 LEU A 128     2834   2967   3332   -156   -242   -176       C  
ATOM   1058  CD2 LEU A 128      11.990  28.874  44.021  1.00 28.77           C  
ANISOU 1058  CD2 LEU A 128     3456   3624   3850   -116   -288   -177       C  
ATOM   1059  N   VAL A 129       8.852  33.298  43.958  1.00 21.91           N  
ANISOU 1059  N   VAL A 129     2628   2670   3027   -207   -260   -255       N  
ATOM   1060  CA  VAL A 129       8.469  34.650  44.384  1.00 28.24           C  
ANISOU 1060  CA  VAL A 129     3423   3457   3850   -228   -259   -291       C  
ATOM   1061  C   VAL A 129       7.777  34.591  45.747  1.00 25.17           C  
ANISOU 1061  C   VAL A 129     3048   3099   3416   -216   -285   -312       C  
ATOM   1062  O   VAL A 129       8.090  35.356  46.666  1.00 26.58           O  
ANISOU 1062  O   VAL A 129     3206   3294   3600   -225   -305   -358       O  
ATOM   1063  CB  VAL A 129       7.566  35.307  43.316  1.00 25.16           C  
ANISOU 1063  CB  VAL A 129     3057   3023   3482   -241   -223   -270       C  
ATOM   1064  CG1 VAL A 129       6.969  36.641  43.833  1.00 26.99           C  
ANISOU 1064  CG1 VAL A 129     3288   3235   3732   -258   -219   -302       C  
ATOM   1065  CG2 VAL A 129       8.350  35.543  42.022  1.00 23.56           C  
ANISOU 1065  CG2 VAL A 129     2838   2792   3324   -252   -196   -252       C  
ATOM   1066  N   VAL A 130       6.872  33.634  45.910  1.00 23.74           N  
ANISOU 1066  N   VAL A 130     2900   2928   3191   -195   -284   -280       N  
ATOM   1067  CA  VAL A 130       6.159  33.465  47.178  1.00 24.37           C  
ANISOU 1067  CA  VAL A 130     2997   3037   3225   -179   -302   -292       C  
ATOM   1068  C   VAL A 130       7.132  33.138  48.312  1.00 26.32           C  
ANISOU 1068  C   VAL A 130     3219   3335   3446   -161   -337   -316       C  
ATOM   1069  O   VAL A 130       7.083  33.743  49.393  1.00 26.25           O  
ANISOU 1069  O   VAL A 130     3202   3351   3419   -161   -359   -356       O  
ATOM   1070  CB  VAL A 130       5.071  32.386  47.026  1.00 24.64           C  
ANISOU 1070  CB  VAL A 130     3069   3068   3224   -160   -287   -249       C  
ATOM   1071  CG1 VAL A 130       4.408  32.119  48.375  1.00 29.87           C  
ANISOU 1071  CG1 VAL A 130     3748   3762   3838   -140   -301   -256       C  
ATOM   1072  CG2 VAL A 130       4.026  32.840  46.012  1.00 31.69           C  
ANISOU 1072  CG2 VAL A 130     3982   3921   4138   -176   -258   -233       C  
ATOM   1073  N   LEU A 131       8.051  32.197  48.077  1.00 26.82           N  
ANISOU 1073  N   LEU A 131     3268   3415   3507   -145   -345   -295       N  
ATOM   1074  CA  LEU A 131       9.035  31.855  49.107  1.00 27.04           C  
ANISOU 1074  CA  LEU A 131     3269   3497   3509   -123   -380   -314       C  
ATOM   1075  C   LEU A 131       9.957  33.024  49.415  1.00 28.77           C  
ANISOU 1075  C   LEU A 131     3442   3727   3761   -147   -402   -373       C  
ATOM   1076  O   LEU A 131      10.327  33.236  50.577  1.00 27.70           O  
ANISOU 1076  O   LEU A 131     3288   3640   3598   -135   -436   -411       O  
ATOM   1077  CB  LEU A 131       9.857  30.634  48.680  1.00 27.50           C  
ANISOU 1077  CB  LEU A 131     3318   3566   3564    -99   -379   -276       C  
ATOM   1078  CG  LEU A 131       9.099  29.308  48.739  1.00 33.29           C  
ANISOU 1078  CG  LEU A 131     4092   4299   4259    -69   -363   -225       C  
ATOM   1079  CD1 LEU A 131       9.935  28.171  48.145  1.00 35.65           C  
ANISOU 1079  CD1 LEU A 131     4382   4598   4566    -49   -354   -189       C  
ATOM   1080  CD2 LEU A 131       8.704  29.001  50.178  1.00 35.42           C  
ANISOU 1080  CD2 LEU A 131     4374   4614   4471    -38   -384   -228       C  
ATOM   1081  N   ALA A 132      10.357  33.788  48.397  1.00 24.77           N  
ANISOU 1081  N   ALA A 132     2917   3179   3316   -179   -381   -383       N  
ATOM   1082  CA  ALA A 132      11.235  34.930  48.659  1.00 26.16           C  
ANISOU 1082  CA  ALA A 132     3048   3359   3534   -207   -395   -442       C  
ATOM   1083  C   ALA A 132      10.540  35.960  49.543  1.00 31.58           C  
ANISOU 1083  C   ALA A 132     3741   4047   4212   -221   -404   -490       C  
ATOM   1084  O   ALA A 132      11.153  36.527  50.460  1.00 28.90           O  
ANISOU 1084  O   ALA A 132     3367   3741   3871   -227   -435   -547       O  
ATOM   1085  CB  ALA A 132      11.682  35.574  47.341  1.00 32.76           C  
ANISOU 1085  CB  ALA A 132     3868   4141   4441   -238   -361   -436       C  
ATOM   1086  N   ILE A 133       9.256  36.219  49.273  1.00 29.38           N  
ANISOU 1086  N   ILE A 133     3503   3732   3927   -225   -377   -469       N  
ATOM   1087  CA  ILE A 133       8.473  37.123  50.119  1.00 32.86           C  
ANISOU 1087  CA  ILE A 133     3956   4173   4356   -234   -381   -510       C  
ATOM   1088  C   ILE A 133       8.333  36.547  51.521  1.00 33.36           C  
ANISOU 1088  C   ILE A 133     4026   4300   4350   -202   -417   -524       C  
ATOM   1089  O   ILE A 133       8.505  37.255  52.523  1.00 33.64           O  
ANISOU 1089  O   ILE A 133     4044   4363   4374   -208   -440   -583       O  
ATOM   1090  CB  ILE A 133       7.100  37.392  49.472  1.00 32.61           C  
ANISOU 1090  CB  ILE A 133     3967   4093   4332   -239   -343   -476       C  
ATOM   1091  CG1 ILE A 133       7.270  38.188  48.172  1.00 33.67           C  
ANISOU 1091  CG1 ILE A 133     4092   4169   4534   -267   -307   -467       C  
ATOM   1092  CG2 ILE A 133       6.142  38.086  50.446  1.00 34.12           C  
ANISOU 1092  CG2 ILE A 133     4176   4289   4500   -239   -346   -509       C  
ATOM   1093  CD1 ILE A 133       5.976  38.306  47.382  1.00 37.77           C  
ANISOU 1093  CD1 ILE A 133     4649   4647   5055   -266   -272   -425       C  
ATOM   1094  N   GLU A 134       8.043  35.247  51.616  1.00 26.44           N  
ANISOU 1094  N   GLU A 134     3175   3447   3424   -168   -420   -473       N  
ATOM   1095  CA  GLU A 134       7.897  34.619  52.923  1.00 33.61           C  
ANISOU 1095  CA  GLU A 134     4093   4415   4262   -131   -448   -476       C  
ATOM   1096  C   GLU A 134       9.182  34.726  53.738  1.00 33.10           C  
ANISOU 1096  C   GLU A 134     3982   4409   4184   -122   -492   -522       C  
ATOM   1097  O   GLU A 134       9.150  35.088  54.916  1.00 34.48           O  
ANISOU 1097  O   GLU A 134     4150   4631   4318   -111   -520   -566       O  
ATOM   1098  CB  GLU A 134       7.468  33.157  52.755  1.00 30.85           C  
ANISOU 1098  CB  GLU A 134     3776   4072   3874    -96   -436   -407       C  
ATOM   1099  CG  GLU A 134       7.174  32.440  54.075  1.00 28.94           C  
ANISOU 1099  CG  GLU A 134     3551   3887   3558    -53   -455   -398       C  
ATOM   1100  CD  GLU A 134       8.340  31.605  54.566  1.00 35.87           C  
ANISOU 1100  CD  GLU A 134     4403   4821   4406    -18   -486   -388       C  
ATOM   1101  OE1 GLU A 134       9.415  31.670  53.938  1.00 40.15           O  
ANISOU 1101  OE1 GLU A 134     4909   5359   4988    -32   -495   -398       O  
ATOM   1102  OE2 GLU A 134       8.191  30.897  55.589  1.00 37.51           O  
ANISOU 1102  OE2 GLU A 134     4625   5077   4550     25   -499   -370       O  
ATOM   1103  N   ARG A 135      10.335  34.429  53.121  1.00 28.54           N  
ANISOU 1103  N   ARG A 135     3369   3835   3640   -127   -500   -516       N  
ATOM   1104  CA  ARG A 135      11.603  34.521  53.858  1.00 27.72           C  
ANISOU 1104  CA  ARG A 135     3214   3791   3527   -118   -544   -562       C  
ATOM   1105  C   ARG A 135      11.891  35.948  54.288  1.00 35.24           C  
ANISOU 1105  C   ARG A 135     4132   4744   4513   -156   -559   -645       C  
ATOM   1106  O   ARG A 135      12.381  36.184  55.405  1.00 37.40           O  
ANISOU 1106  O   ARG A 135     4378   5081   4752   -144   -601   -699       O  
ATOM   1107  CB  ARG A 135      12.764  34.019  53.001  1.00 34.43           C  
ANISOU 1107  CB  ARG A 135     4028   4635   4417   -120   -544   -540       C  
ATOM   1108  CG  ARG A 135      12.786  32.527  52.736  1.00 34.63           C  
ANISOU 1108  CG  ARG A 135     4076   4672   4408    -78   -535   -468       C  
ATOM   1109  CD  ARG A 135      13.191  31.778  53.997  1.00 35.88           C  
ANISOU 1109  CD  ARG A 135     4225   4912   4497    -27   -576   -466       C  
ATOM   1110  NE  ARG A 135      12.011  31.437  54.779  1.00 32.43           N  
ANISOU 1110  NE  ARG A 135     3837   4486   3998     -1   -570   -445       N  
ATOM   1111  CZ  ARG A 135      12.025  31.095  56.058  1.00 35.37           C  
ANISOU 1111  CZ  ARG A 135     4211   4927   4300     41   -601   -452       C  
ATOM   1112  NH1 ARG A 135      13.152  31.041  56.747  1.00 33.41           N  
ANISOU 1112  NH1 ARG A 135     3917   4749   4029     63   -646   -482       N  
ATOM   1113  NH2 ARG A 135      10.875  30.794  56.656  1.00 34.45           N  
ANISOU 1113  NH2 ARG A 135     4143   4813   4133     62   -586   -426       N  
ATOM   1114  N   TYR A 136      11.608  36.911  53.405  1.00 31.00           N  
ANISOU 1114  N   TYR A 136     3596   4137   4044   -199   -524   -658       N  
ATOM   1115  CA  TYR A 136      11.832  38.316  53.725  1.00 34.32           C  
ANISOU 1115  CA  TYR A 136     3987   4545   4509   -239   -528   -737       C  
ATOM   1116  C   TYR A 136      10.972  38.750  54.907  1.00 41.35           C  
ANISOU 1116  C   TYR A 136     4901   5463   5349   -229   -542   -775       C  
ATOM   1117  O   TYR A 136      11.444  39.462  55.800  1.00 42.00           O  
ANISOU 1117  O   TYR A 136     4950   5582   5427   -241   -572   -852       O  
ATOM   1118  CB  TYR A 136      11.534  39.179  52.498  1.00 37.11           C  
ANISOU 1118  CB  TYR A 136     4346   4811   4942   -280   -477   -727       C  
ATOM   1119  CG  TYR A 136      11.348  40.650  52.810  1.00 42.64           C  
ANISOU 1119  CG  TYR A 136     5033   5480   5688   -318   -466   -797       C  
ATOM   1120  CD1 TYR A 136      12.435  41.457  53.121  1.00 44.43           C  
ANISOU 1120  CD1 TYR A 136     5202   5717   5963   -349   -483   -872       C  
ATOM   1121  CD2 TYR A 136      10.087  41.228  52.798  1.00 49.34           C  
ANISOU 1121  CD2 TYR A 136     5924   6287   6536   -324   -435   -790       C  
ATOM   1122  CE1 TYR A 136      12.271  42.800  53.410  1.00 43.70           C  
ANISOU 1122  CE1 TYR A 136     5095   5589   5918   -387   -468   -940       C  
ATOM   1123  CE2 TYR A 136       9.911  42.573  53.084  1.00 57.10           C  
ANISOU 1123  CE2 TYR A 136     6896   7236   7565   -358   -420   -854       C  
ATOM   1124  CZ  TYR A 136      11.010  43.350  53.385  1.00 50.36           C  
ANISOU 1124  CZ  TYR A 136     5986   6389   6760   -390   -435   -930       C  
ATOM   1125  OH  TYR A 136      10.843  44.683  53.672  1.00 62.41           O  
ANISOU 1125  OH  TYR A 136     7499   7875   8337   -425   -416   -997       O  
ATOM   1126  N   VAL A 137       9.701  38.332  54.922  1.00 40.42           N  
ANISOU 1126  N   VAL A 137     4839   5328   5192   -209   -519   -727       N  
ATOM   1127  CA  VAL A 137       8.818  38.645  56.044  1.00 39.20           C  
ANISOU 1127  CA  VAL A 137     4710   5200   4983   -195   -528   -756       C  
ATOM   1128  C   VAL A 137       9.322  37.993  57.332  1.00 46.39           C  
ANISOU 1128  C   VAL A 137     5608   6203   5815   -154   -578   -775       C  
ATOM   1129  O   VAL A 137       9.439  38.652  58.375  1.00 47.63           O  
ANISOU 1129  O   VAL A 137     5749   6402   5945   -156   -606   -845       O  
ATOM   1130  CB  VAL A 137       7.378  38.204  55.715  1.00 43.10           C  
ANISOU 1130  CB  VAL A 137     5263   5658   5455   -180   -491   -692       C  
ATOM   1131  CG1 VAL A 137       6.523  38.191  56.977  1.00 46.43           C  
ANISOU 1131  CG1 VAL A 137     5714   6120   5808   -154   -502   -709       C  
ATOM   1132  CG2 VAL A 137       6.782  39.118  54.674  1.00 39.11           C  
ANISOU 1132  CG2 VAL A 137     4768   5071   5020   -217   -447   -687       C  
ATOM   1133  N   VAL A 138       9.632  36.691  57.284  1.00 39.85           N  
ANISOU 1133  N   VAL A 138     4786   5408   4946   -115   -589   -715       N  
ATOM   1134  CA  VAL A 138      10.000  35.978  58.510  1.00 38.71           C  
ANISOU 1134  CA  VAL A 138     4636   5353   4719    -66   -631   -720       C  
ATOM   1135  C   VAL A 138      11.326  36.488  59.063  1.00 45.98           C  
ANISOU 1135  C   VAL A 138     5493   6332   5645    -74   -680   -795       C  
ATOM   1136  O   VAL A 138      11.466  36.711  60.270  1.00 53.86           O  
ANISOU 1136  O   VAL A 138     6478   7400   6585    -54   -718   -846       O  
ATOM   1137  CB  VAL A 138      10.054  34.457  58.273  1.00 45.75           C  
ANISOU 1137  CB  VAL A 138     5549   6261   5575    -20   -625   -634       C  
ATOM   1138  CG1 VAL A 138      10.709  33.760  59.478  1.00 46.10           C  
ANISOU 1138  CG1 VAL A 138     5576   6402   5539     34   -671   -638       C  
ATOM   1139  CG2 VAL A 138       8.675  33.903  58.045  1.00 41.12           C  
ANISOU 1139  CG2 VAL A 138     5023   5633   4969     -7   -582   -571       C  
ATOM   1140  N   VAL A 139      12.327  36.655  58.198  1.00 44.75           N  
ANISOU 1140  N   VAL A 139     5294   6152   5558   -103   -681   -804       N  
ATOM   1141  CA  VAL A 139      13.659  37.015  58.675  1.00 48.55           C  
ANISOU 1141  CA  VAL A 139     5707   6691   6048   -109   -729   -872       C  
ATOM   1142  C   VAL A 139      13.732  38.498  59.020  1.00 58.71           C  
ANISOU 1142  C   VAL A 139     6966   7965   7378   -159   -736   -971       C  
ATOM   1143  O   VAL A 139      14.227  38.875  60.088  1.00 62.14           O  
ANISOU 1143  O   VAL A 139     7365   8471   7776   -152   -782  -1044       O  
ATOM   1144  CB  VAL A 139      14.723  36.634  57.629  1.00 49.03           C  
ANISOU 1144  CB  VAL A 139     5729   6730   6169   -122   -723   -844       C  
ATOM   1145  CG1 VAL A 139      16.109  37.110  58.077  1.00 48.80           C  
ANISOU 1145  CG1 VAL A 139     5622   6758   6161   -135   -771   -922       C  
ATOM   1146  CG2 VAL A 139      14.724  35.133  57.384  1.00 43.91           C  
ANISOU 1146  CG2 VAL A 139     5107   6099   5478    -70   -718   -753       C  
ATOM   1147  N   CYS A 140      13.262  39.362  58.115  1.00 57.83           N  
ANISOU 1147  N   CYS A 140     6865   7762   7343   -207   -688   -976       N  
ATOM   1148  CA  CYS A 140      13.397  40.804  58.292  1.00 50.64           C  
ANISOU 1148  CA  CYS A 140     5926   6824   6492   -259   -684  -1068       C  
ATOM   1149  C   CYS A 140      12.273  41.424  59.104  1.00 64.60           C  
ANISOU 1149  C   CYS A 140     7733   8590   8223   -258   -676  -1101       C  
ATOM   1150  O   CYS A 140      12.382  42.599  59.473  1.00 72.63           O  
ANISOU 1150  O   CYS A 140     8725   9593   9277   -295   -677  -1187       O  
ATOM   1151  CB  CYS A 140      13.480  41.501  56.937  1.00 53.55           C  
ANISOU 1151  CB  CYS A 140     6287   7094   6966   -308   -632  -1055       C  
ATOM   1152  SG  CYS A 140      15.008  41.145  56.067  1.00 55.92           S  
ANISOU 1152  SG  CYS A 140     6524   7395   7327   -322   -640  -1045       S  
ATOM   1153  N   LYS A 141      11.214  40.670  59.391  1.00 59.67           N  
ANISOU 1153  N   LYS A 141     7167   7976   7528   -216   -666  -1038       N  
ATOM   1154  CA  LYS A 141      10.088  41.093  60.219  1.00 63.01           C  
ANISOU 1154  CA  LYS A 141     7631   8404   7905   -207   -657  -1061       C  
ATOM   1155  C   LYS A 141       9.692  42.549  59.935  1.00 75.18           C  
ANISOU 1155  C   LYS A 141     9169   9873   9523   -260   -622  -1121       C  
ATOM   1156  O   LYS A 141       9.781  43.402  60.824  1.00 82.45           O  
ANISOU 1156  O   LYS A 141    10072  10819  10436   -275   -641  -1209       O  
ATOM   1157  CB  LYS A 141      10.396  40.886  61.699  1.00 72.19           C  
ANISOU 1157  CB  LYS A 141     8781   9671   8978   -170   -711  -1112       C  
ATOM   1158  CG  LYS A 141      10.699  39.432  62.046  1.00 72.09           C  
ANISOU 1158  CG  LYS A 141     8776   9729   8886   -109   -740  -1045       C  
ATOM   1159  CD  LYS A 141      11.230  39.278  63.459  1.00 77.39           C  
ANISOU 1159  CD  LYS A 141     9424  10512   9470    -70   -799  -1099       C  
ATOM   1160  CE  LYS A 141      11.455  37.809  63.803  1.00 84.34           C  
ANISOU 1160  CE  LYS A 141    10317  11459  10270     -3   -819  -1021       C  
ATOM   1161  NZ  LYS A 141      12.410  37.134  62.872  1.00 72.47           N  
ANISOU 1161  NZ  LYS A 141     8782   9942   8812     -4   -822   -975       N  
ATOM   1162  N   PRO A 142       9.269  42.865  58.698  1.00 74.52           N  
ANISOU 1162  N   PRO A 142     9102   9699   9514   -288   -571  -1076       N  
ATOM   1163  CA  PRO A 142       8.877  44.237  58.366  1.00 76.50           C  
ANISOU 1163  CA  PRO A 142     9352   9874   9840   -334   -531  -1123       C  
ATOM   1164  C   PRO A 142       7.535  44.624  58.983  1.00 74.93           C  
ANISOU 1164  C   PRO A 142     9201   9663   9605   -322   -510  -1128       C  
ATOM   1165  O   PRO A 142       7.512  45.402  59.939  1.00 81.36           O  
ANISOU 1165  O   PRO A 142    10005  10500  10408   -332   -524  -1210       O  
ATOM   1166  CB  PRO A 142       8.788  44.210  56.838  1.00 69.73           C  
ANISOU 1166  CB  PRO A 142     8503   8936   9055   -352   -483  -1053       C  
ATOM   1167  CG  PRO A 142       8.385  42.816  56.529  1.00 70.22           C  
ANISOU 1167  CG  PRO A 142     8600   9022   9058   -310   -488   -961       C  
ATOM   1168  CD  PRO A 142       9.082  41.953  57.553  1.00 69.80           C  
ANISOU 1168  CD  PRO A 142     8528   9065   8929   -275   -544   -978       C  
ATOM   1169  N   ARG A 147       2.271  37.785  60.650  1.00 65.94           N  
ANISOU 1169  N   ARG A 147     8333   8676   8046    -50   -468   -691       N  
ATOM   1170  CA  ARG A 147       3.215  36.722  60.327  1.00 74.66           C  
ANISOU 1170  CA  ARG A 147     9420   9808   9139    -31   -489   -650       C  
ATOM   1171  C   ARG A 147       2.685  35.837  59.197  1.00 74.94           C  
ANISOU 1171  C   ARG A 147     9478   9792   9205    -31   -453   -570       C  
ATOM   1172  O   ARG A 147       1.485  35.558  59.120  1.00 79.82           O  
ANISOU 1172  O   ARG A 147    10132  10382   9814    -24   -419   -530       O  
ATOM   1173  CB  ARG A 147       3.516  35.877  61.568  1.00 65.94           C  
ANISOU 1173  CB  ARG A 147     8322   8788   7945     23   -518   -642       C  
ATOM   1174  N   PHE A 148       3.595  35.399  58.328  1.00 68.65           N  
ANISOU 1174  N   PHE A 148     8657   8982   8443    -41   -461   -548       N  
ATOM   1175  CA  PHE A 148       3.252  34.577  57.169  1.00 55.07           C  
ANISOU 1175  CA  PHE A 148     6953   7215   6754    -44   -431   -480       C  
ATOM   1176  C   PHE A 148       2.854  33.178  57.636  1.00 61.10           C  
ANISOU 1176  C   PHE A 148     7746   8008   7462      1   -422   -419       C  
ATOM   1177  O   PHE A 148       3.713  32.375  58.016  1.00 66.18           O  
ANISOU 1177  O   PHE A 148     8377   8695   8072     32   -445   -403       O  
ATOM   1178  CB  PHE A 148       4.441  34.527  56.211  1.00 54.31           C  
ANISOU 1178  CB  PHE A 148     6822   7105   6708    -64   -443   -481       C  
ATOM   1179  CG  PHE A 148       4.063  34.255  54.786  1.00 42.03           C  
ANISOU 1179  CG  PHE A 148     5278   5488   5204    -84   -408   -435       C  
ATOM   1180  CD1 PHE A 148       3.665  32.990  54.394  1.00 45.05           C  
ANISOU 1180  CD1 PHE A 148     5685   5862   5570    -62   -390   -371       C  
ATOM   1181  CD2 PHE A 148       4.120  35.261  53.836  1.00 44.20           C  
ANISOU 1181  CD2 PHE A 148     5539   5712   5544   -124   -393   -456       C  
ATOM   1182  CE1 PHE A 148       3.315  32.730  53.074  1.00 41.39           C  
ANISOU 1182  CE1 PHE A 148     5231   5347   5150    -81   -360   -335       C  
ATOM   1183  CE2 PHE A 148       3.769  35.005  52.511  1.00 48.12           C  
ANISOU 1183  CE2 PHE A 148     6046   6157   6080   -138   -363   -413       C  
ATOM   1184  CZ  PHE A 148       3.363  33.737  52.136  1.00 42.18           C  
ANISOU 1184  CZ  PHE A 148     5316   5403   5305   -117   -349   -355       C  
ATOM   1185  N   GLY A 149       1.551  32.879  57.610  1.00 54.57           N  
ANISOU 1185  N   GLY A 149     6956   7152   6625      6   -387   -384       N  
ATOM   1186  CA  GLY A 149       1.025  31.630  58.098  1.00 54.48           C  
ANISOU 1186  CA  GLY A 149     6974   7159   6566     46   -370   -327       C  
ATOM   1187  C   GLY A 149       0.470  30.746  56.999  1.00 47.21           C  
ANISOU 1187  C   GLY A 149     6070   6187   5682     38   -334   -270       C  
ATOM   1188  O   GLY A 149       0.767  30.919  55.810  1.00 47.11           O  
ANISOU 1188  O   GLY A 149     6043   6135   5723      7   -330   -268       O  
ATOM   1189  N   GLU A 150      -0.353  29.773  57.408  1.00 48.26           N  
ANISOU 1189  N   GLU A 150     6233   6321   5784     65   -306   -222       N  
ATOM   1190  CA  GLU A 150      -0.925  28.833  56.447  1.00 50.56           C  
ANISOU 1190  CA  GLU A 150     6539   6565   6107     57   -270   -172       C  
ATOM   1191  C   GLU A 150      -1.830  29.546  55.458  1.00 42.56           C  
ANISOU 1191  C   GLU A 150     5527   5500   5145     16   -251   -184       C  
ATOM   1192  O   GLU A 150      -1.841  29.209  54.268  1.00 46.82           O  
ANISOU 1192  O   GLU A 150     6061   6001   5725     -5   -239   -165       O  
ATOM   1193  CB  GLU A 150      -1.704  27.722  57.162  1.00 48.00           C  
ANISOU 1193  CB  GLU A 150     6245   6248   5745     92   -238   -123       C  
ATOM   1194  CG  GLU A 150      -0.850  26.780  57.978  1.00 57.31           C  
ANISOU 1194  CG  GLU A 150     7426   7472   6876    141   -248    -94       C  
ATOM   1195  CD  GLU A 150      -1.605  25.545  58.456  1.00 55.76           C  
ANISOU 1195  CD  GLU A 150     7261   7268   6656    174   -205    -35       C  
ATOM   1196  OE1 GLU A 150      -2.273  24.885  57.630  1.00 48.76           O  
ANISOU 1196  OE1 GLU A 150     6385   6331   5812    156   -168     -5       O  
ATOM   1197  OE2 GLU A 150      -1.524  25.235  59.664  1.00 64.69           O  
ANISOU 1197  OE2 GLU A 150     8405   8446   7728    219   -206    -19       O  
ATOM   1198  N   ASN A 151      -2.607  30.529  55.937  1.00 43.92           N  
ANISOU 1198  N   ASN A 151     5705   5671   5310      7   -248   -214       N  
ATOM   1199  CA  ASN A 151      -3.524  31.250  55.057  1.00 43.01           C  
ANISOU 1199  CA  ASN A 151     5591   5511   5241    -26   -229   -222       C  
ATOM   1200  C   ASN A 151      -2.780  31.952  53.943  1.00 41.21           C  
ANISOU 1200  C   ASN A 151     5339   5258   5062    -57   -243   -243       C  
ATOM   1201  O   ASN A 151      -3.257  31.996  52.806  1.00 39.95           O  
ANISOU 1201  O   ASN A 151     5178   5060   4942    -78   -226   -228       O  
ATOM   1202  CB  ASN A 151      -4.316  32.293  55.841  1.00 48.47           C  
ANISOU 1202  CB  ASN A 151     6291   6208   5919    -28   -224   -256       C  
ATOM   1203  CG  ASN A 151      -5.427  31.692  56.657  1.00 57.01           C  
ANISOU 1203  CG  ASN A 151     7398   7298   6965     -4   -196   -229       C  
ATOM   1204  OD1 ASN A 151      -5.850  30.561  56.412  1.00 58.60           O  
ANISOU 1204  OD1 ASN A 151     7612   7488   7166      6   -173   -184       O  
ATOM   1205  ND2 ASN A 151      -5.914  32.448  57.636  1.00 59.05           N  
ANISOU 1205  ND2 ASN A 151     7665   7574   7196      5   -195   -258       N  
ATOM   1206  N   HIS A 152      -1.651  32.581  54.276  1.00 32.29           N  
ANISOU 1206  N   HIS A 152     4187   4151   3930    -60   -274   -281       N  
ATOM   1207  CA  HIS A 152      -0.876  33.278  53.259  1.00 44.89           C  
ANISOU 1207  CA  HIS A 152     5758   5722   5577    -89   -283   -301       C  
ATOM   1208  C   HIS A 152      -0.227  32.293  52.313  1.00 32.33           C  
ANISOU 1208  C   HIS A 152     4160   4121   4002    -88   -281   -264       C  
ATOM   1209  O   HIS A 152      -0.077  32.578  51.119  1.00 33.57           O  
ANISOU 1209  O   HIS A 152     4308   4245   4203   -111   -272   -259       O  
ATOM   1210  CB  HIS A 152       0.192  34.145  53.907  1.00 47.15           C  
ANISOU 1210  CB  HIS A 152     6018   6037   5861    -94   -314   -354       C  
ATOM   1211  CG  HIS A 152      -0.354  35.083  54.927  1.00 54.26           C  
ANISOU 1211  CG  HIS A 152     6925   6950   6742    -93   -317   -397       C  
ATOM   1212  ND1 HIS A 152      -0.340  34.801  56.273  1.00 51.04           N  
ANISOU 1212  ND1 HIS A 152     6525   6594   6273    -63   -333   -411       N  
ATOM   1213  CD2 HIS A 152      -0.959  36.286  54.797  1.00 59.40           C  
ANISOU 1213  CD2 HIS A 152     7576   7570   7424   -115   -303   -428       C  
ATOM   1214  CE1 HIS A 152      -0.905  35.795  56.933  1.00 69.34           C  
ANISOU 1214  CE1 HIS A 152     8849   8912   8586    -69   -330   -453       C  
ATOM   1215  NE2 HIS A 152      -1.291  36.709  56.060  1.00 69.71           N  
ANISOU 1215  NE2 HIS A 152     8890   8906   8689   -102   -310   -464       N  
ATOM   1216  N   ALA A 153       0.205  31.151  52.850  1.00 36.35           N  
ANISOU 1216  N   ALA A 153     4675   4661   4476    -59   -288   -239       N  
ATOM   1217  CA  ALA A 153       0.822  30.128  52.019  1.00 36.59           C  
ANISOU 1217  CA  ALA A 153     4700   4681   4521    -55   -283   -205       C  
ATOM   1218  C   ALA A 153      -0.168  29.581  51.001  1.00 37.16           C  
ANISOU 1218  C   ALA A 153     4790   4711   4616    -68   -250   -171       C  
ATOM   1219  O   ALA A 153       0.174  29.388  49.828  1.00 33.35           O  
ANISOU 1219  O   ALA A 153     4300   4204   4167    -83   -243   -160       O  
ATOM   1220  CB  ALA A 153       1.364  29.004  52.905  1.00 31.85           C  
ANISOU 1220  CB  ALA A 153     4105   4120   3877    -15   -292   -180       C  
ATOM   1221  N   ILE A 154      -1.399  29.305  51.440  1.00 33.49           N  
ANISOU 1221  N   ILE A 154     4349   4241   4133    -60   -229   -157       N  
ATOM   1222  CA  ILE A 154      -2.402  28.773  50.528  1.00 30.69           C  
ANISOU 1222  CA  ILE A 154     4008   3852   3802    -73   -200   -131       C  
ATOM   1223  C   ILE A 154      -2.792  29.830  49.507  1.00 32.68           C  
ANISOU 1223  C   ILE A 154     4250   4077   4090   -103   -198   -149       C  
ATOM   1224  O   ILE A 154      -2.980  29.531  48.318  1.00 28.82           O  
ANISOU 1224  O   ILE A 154     3758   3564   3627   -117   -186   -135       O  
ATOM   1225  CB  ILE A 154      -3.611  28.245  51.324  1.00 34.29           C  
ANISOU 1225  CB  ILE A 154     4486   4310   4232    -59   -176   -113       C  
ATOM   1226  CG1 ILE A 154      -3.185  27.030  52.164  1.00 36.11           C  
ANISOU 1226  CG1 ILE A 154     4728   4562   4429    -25   -170    -83       C  
ATOM   1227  CG2 ILE A 154      -4.764  27.883  50.375  1.00 37.11           C  
ANISOU 1227  CG2 ILE A 154     4850   4633   4618    -78   -148    -97       C  
ATOM   1228  CD1 ILE A 154      -4.139  26.669  53.298  1.00 39.03           C  
ANISOU 1228  CD1 ILE A 154     5120   4944   4766     -3   -148    -67       C  
ATOM   1229  N   MET A 155      -2.921  31.088  49.945  1.00 28.39           N  
ANISOU 1229  N   MET A 155     3701   3538   3550   -111   -208   -181       N  
ATOM   1230  CA  MET A 155      -3.168  32.147  48.973  1.00 32.83           C  
ANISOU 1230  CA  MET A 155     4253   4072   4150   -134   -203   -193       C  
ATOM   1231  C   MET A 155      -1.997  32.262  48.003  1.00 29.02           C  
ANISOU 1231  C   MET A 155     3751   3579   3695   -146   -212   -195       C  
ATOM   1232  O   MET A 155      -2.193  32.530  46.813  1.00 32.48           O  
ANISOU 1232  O   MET A 155     4186   3993   4161   -160   -200   -185       O  
ATOM   1233  CB  MET A 155      -3.419  33.483  49.682  1.00 31.14           C  
ANISOU 1233  CB  MET A 155     4035   3858   3937   -139   -208   -229       C  
ATOM   1234  CG  MET A 155      -3.929  34.566  48.755  1.00 40.63           C  
ANISOU 1234  CG  MET A 155     5231   5028   5179   -158   -194   -234       C  
ATOM   1235  SD  MET A 155      -4.141  36.128  49.610  1.00 60.15           S  
ANISOU 1235  SD  MET A 155     7699   7494   7660   -164   -194   -279       S  
ATOM   1236  CE  MET A 155      -4.232  35.548  51.297  1.00 41.72           C  
ANISOU 1236  CE  MET A 155     5378   5202   5270   -141   -207   -293       C  
ATOM   1237  N   GLY A 156      -0.770  32.058  48.501  1.00 30.19           N  
ANISOU 1237  N   GLY A 156     3887   3750   3835   -138   -232   -206       N  
ATOM   1238  CA  GLY A 156       0.382  32.054  47.615  1.00 27.61           C  
ANISOU 1238  CA  GLY A 156     3540   3415   3536   -148   -238   -205       C  
ATOM   1239  C   GLY A 156       0.292  30.958  46.571  1.00 27.04           C  
ANISOU 1239  C   GLY A 156     3476   3329   3469   -146   -222   -170       C  
ATOM   1240  O   GLY A 156       0.573  31.192  45.391  1.00 28.94           O  
ANISOU 1240  O   GLY A 156     3708   3548   3738   -160   -213   -164       O  
ATOM   1241  N   VAL A 157      -0.131  29.758  46.985  1.00 27.97           N  
ANISOU 1241  N   VAL A 157     3611   3457   3560   -129   -215   -147       N  
ATOM   1242  CA  VAL A 157      -0.290  28.649  46.041  1.00 29.10           C  
ANISOU 1242  CA  VAL A 157     3762   3584   3710   -129   -197   -119       C  
ATOM   1243  C   VAL A 157      -1.286  29.010  44.943  1.00 30.28           C  
ANISOU 1243  C   VAL A 157     3916   3709   3878   -147   -181   -116       C  
ATOM   1244  O   VAL A 157      -1.025  28.814  43.747  1.00 27.57           O  
ANISOU 1244  O   VAL A 157     3570   3353   3554   -156   -173   -107       O  
ATOM   1245  CB  VAL A 157      -0.720  27.372  46.783  1.00 29.03           C  
ANISOU 1245  CB  VAL A 157     3772   3584   3675   -108   -186    -96       C  
ATOM   1246  CG1 VAL A 157      -1.229  26.295  45.784  1.00 26.94           C  
ANISOU 1246  CG1 VAL A 157     3517   3295   3424   -114   -161    -74       C  
ATOM   1247  CG2 VAL A 157       0.425  26.828  47.626  1.00 30.68           C  
ANISOU 1247  CG2 VAL A 157     3974   3818   3864    -83   -201    -90       C  
ATOM   1248  N   ALA A 158      -2.457  29.527  45.331  1.00 30.69           N  
ANISOU 1248  N   ALA A 158     3977   3759   3924   -150   -175   -121       N  
ATOM   1249  CA  ALA A 158      -3.462  29.867  44.328  1.00 26.09           C  
ANISOU 1249  CA  ALA A 158     3396   3160   3356   -164   -162   -117       C  
ATOM   1250  C   ALA A 158      -2.926  30.930  43.380  1.00 22.76           C  
ANISOU 1250  C   ALA A 158     2961   2727   2959   -174   -165   -124       C  
ATOM   1251  O   ALA A 158      -3.190  30.901  42.177  1.00 25.33           O  
ANISOU 1251  O   ALA A 158     3285   3044   3296   -180   -156   -113       O  
ATOM   1252  CB  ALA A 158      -4.741  30.359  45.009  1.00 27.95           C  
ANISOU 1252  CB  ALA A 158     3640   3397   3583   -162   -156   -123       C  
ATOM   1253  N   PHE A 159      -2.161  31.868  43.921  1.00 20.89           N  
ANISOU 1253  N   PHE A 159     2713   2491   2732   -176   -176   -143       N  
ATOM   1254  CA  PHE A 159      -1.560  32.921  43.123  1.00 25.65           C  
ANISOU 1254  CA  PHE A 159     3302   3078   3365   -187   -173   -149       C  
ATOM   1255  C   PHE A 159      -0.635  32.344  42.058  1.00 30.01           C  
ANISOU 1255  C   PHE A 159     3847   3626   3928   -189   -169   -134       C  
ATOM   1256  O   PHE A 159      -0.636  32.812  40.918  1.00 22.96           O  
ANISOU 1256  O   PHE A 159     2952   2720   3053   -194   -156   -123       O  
ATOM   1257  CB  PHE A 159      -0.786  33.857  44.053  1.00 26.52           C  
ANISOU 1257  CB  PHE A 159     3399   3191   3487   -191   -185   -179       C  
ATOM   1258  CG  PHE A 159       0.027  34.878  43.338  1.00 36.59           C  
ANISOU 1258  CG  PHE A 159     4656   4444   4800   -204   -178   -187       C  
ATOM   1259  CD1 PHE A 159      -0.585  35.955  42.748  1.00 30.50           C  
ANISOU 1259  CD1 PHE A 159     3886   3649   4053   -210   -159   -183       C  
ATOM   1260  CD2 PHE A 159       1.412  34.773  43.279  1.00 32.15           C  
ANISOU 1260  CD2 PHE A 159     4075   3887   4255   -209   -187   -196       C  
ATOM   1261  CE1 PHE A 159       0.157  36.913  42.095  1.00 37.30           C  
ANISOU 1261  CE1 PHE A 159     4732   4485   4954   -220   -145   -187       C  
ATOM   1262  CE2 PHE A 159       2.159  35.734  42.632  1.00 37.27           C  
ANISOU 1262  CE2 PHE A 159     4705   4512   4945   -222   -174   -204       C  
ATOM   1263  CZ  PHE A 159       1.522  36.807  42.035  1.00 32.48           C  
ANISOU 1263  CZ  PHE A 159     4101   3876   4362   -228   -151   -198       C  
ATOM   1264  N   THR A 160       0.167  31.325  42.409  1.00 23.83           N  
ANISOU 1264  N   THR A 160     3063   2858   3135   -181   -178   -131       N  
ATOM   1265  CA  THR A 160       1.101  30.781  41.414  1.00 22.19           C  
ANISOU 1265  CA  THR A 160     2848   2645   2939   -182   -172   -118       C  
ATOM   1266  C   THR A 160       0.370  30.154  40.232  1.00 23.77           C  
ANISOU 1266  C   THR A 160     3060   2837   3133   -182   -156   -100       C  
ATOM   1267  O   THR A 160       0.846  30.244  39.093  1.00 22.88           O  
ANISOU 1267  O   THR A 160     2943   2717   3034   -185   -145    -91       O  
ATOM   1268  CB  THR A 160       2.069  29.746  42.019  1.00 20.59           C  
ANISOU 1268  CB  THR A 160     2640   2458   2726   -169   -182   -116       C  
ATOM   1269  OG1 THR A 160       1.370  28.543  42.392  1.00 24.18           O  
ANISOU 1269  OG1 THR A 160     3113   2918   3155   -158   -177   -102       O  
ATOM   1270  CG2 THR A 160       2.859  30.322  43.187  1.00 21.99           C  
ANISOU 1270  CG2 THR A 160     2800   2652   2904   -166   -204   -139       C  
ATOM   1271  N   TRP A 161      -0.770  29.491  40.473  1.00 21.47           N  
ANISOU 1271  N   TRP A 161     2785   2551   2823   -180   -152    -96       N  
ATOM   1272  CA  TRP A 161      -1.549  28.938  39.370  1.00 23.24           C  
ANISOU 1272  CA  TRP A 161     3017   2773   3043   -183   -140    -86       C  
ATOM   1273  C   TRP A 161      -2.128  30.034  38.480  1.00 25.43           C  
ANISOU 1273  C   TRP A 161     3289   3046   3326   -187   -135    -84       C  
ATOM   1274  O   TRP A 161      -2.113  29.918  37.247  1.00 22.75           O  
ANISOU 1274  O   TRP A 161     2950   2708   2987   -186   -126    -76       O  
ATOM   1275  CB  TRP A 161      -2.669  28.048  39.912  1.00 22.72           C  
ANISOU 1275  CB  TRP A 161     2962   2710   2961   -182   -136    -86       C  
ATOM   1276  CG  TRP A 161      -2.156  26.728  40.298  1.00 24.20           C  
ANISOU 1276  CG  TRP A 161     3156   2896   3144   -176   -130    -81       C  
ATOM   1277  CD1 TRP A 161      -1.618  26.363  41.497  1.00 24.39           C  
ANISOU 1277  CD1 TRP A 161     3182   2924   3159   -164   -135    -77       C  
ATOM   1278  CD2 TRP A 161      -2.088  25.589  39.451  1.00 23.21           C  
ANISOU 1278  CD2 TRP A 161     3035   2763   3020   -178   -116    -77       C  
ATOM   1279  NE1 TRP A 161      -1.229  25.033  41.444  1.00 28.61           N  
ANISOU 1279  NE1 TRP A 161     3723   3453   3693   -156   -123    -66       N  
ATOM   1280  CE2 TRP A 161      -1.497  24.548  40.192  1.00 27.17           C  
ANISOU 1280  CE2 TRP A 161     3542   3260   3520   -167   -110    -68       C  
ATOM   1281  CE3 TRP A 161      -2.465  25.352  38.124  1.00 24.81           C  
ANISOU 1281  CE3 TRP A 161     3237   2965   3225   -187   -108    -82       C  
ATOM   1282  CZ2 TRP A 161      -1.296  23.270  39.659  1.00 26.89           C  
ANISOU 1282  CZ2 TRP A 161     3513   3212   3491   -166    -92    -64       C  
ATOM   1283  CZ3 TRP A 161      -2.264  24.093  37.597  1.00 25.46           C  
ANISOU 1283  CZ3 TRP A 161     3325   3039   3311   -189    -93    -84       C  
ATOM   1284  CH2 TRP A 161      -1.694  23.072  38.364  1.00 24.25           C  
ANISOU 1284  CH2 TRP A 161     3179   2875   3162   -179    -83    -75       C  
ATOM   1285  N   VAL A 162      -2.656  31.106  39.078  1.00 20.70           N  
ANISOU 1285  N   VAL A 162     2688   2444   2733   -187   -138    -90       N  
ATOM   1286  CA  VAL A 162      -3.216  32.172  38.261  1.00 24.86           C  
ANISOU 1286  CA  VAL A 162     3212   2966   3268   -186   -130    -82       C  
ATOM   1287  C   VAL A 162      -2.140  32.811  37.392  1.00 27.24           C  
ANISOU 1287  C   VAL A 162     3505   3256   3589   -186   -120    -73       C  
ATOM   1288  O   VAL A 162      -2.341  33.026  36.192  1.00 24.19           O  
ANISOU 1288  O   VAL A 162     3119   2872   3200   -179   -109    -57       O  
ATOM   1289  CB  VAL A 162      -3.937  33.200  39.145  1.00 26.26           C  
ANISOU 1289  CB  VAL A 162     3388   3137   3452   -185   -131    -91       C  
ATOM   1290  CG1 VAL A 162      -4.341  34.405  38.324  1.00 32.61           C  
ANISOU 1290  CG1 VAL A 162     4188   3931   4270   -180   -118    -78       C  
ATOM   1291  CG2 VAL A 162      -5.145  32.521  39.791  1.00 29.85           C  
ANISOU 1291  CG2 VAL A 162     3852   3604   3887   -184   -134    -95       C  
ATOM   1292  N   MET A 163      -0.978  33.127  37.973  1.00 22.41           N  
ANISOU 1292  N   MET A 163     2884   2635   2997   -191   -123    -83       N  
ATOM   1293  CA  MET A 163       0.080  33.731  37.149  1.00 22.45           C  
ANISOU 1293  CA  MET A 163     2878   2626   3027   -193   -110    -75       C  
ATOM   1294  C   MET A 163       0.573  32.768  36.071  1.00 22.56           C  
ANISOU 1294  C   MET A 163     2895   2648   3030   -188   -102    -61       C  
ATOM   1295  O   MET A 163       0.833  33.180  34.933  1.00 25.45           O  
ANISOU 1295  O   MET A 163     3259   3008   3402   -183    -85    -44       O  
ATOM   1296  CB  MET A 163       1.261  34.181  38.023  1.00 22.89           C  
ANISOU 1296  CB  MET A 163     2917   2673   3109   -202   -116    -95       C  
ATOM   1297  CG  MET A 163       0.897  35.291  39.000  1.00 31.38           C  
ANISOU 1297  CG  MET A 163     3988   3737   4199   -209   -120   -116       C  
ATOM   1298  SD  MET A 163       0.034  36.686  38.215  1.00 32.43           S  
ANISOU 1298  SD  MET A 163     4124   3845   4353   -205    -93    -99       S  
ATOM   1299  CE  MET A 163       1.338  37.441  37.293  1.00 33.23           C  
ANISOU 1299  CE  MET A 163     4209   3920   4497   -211    -67    -89       C  
ATOM   1300  N   ALA A 164       0.762  31.494  36.417  1.00 22.20           N  
ANISOU 1300  N   ALA A 164     2853   2614   2967   -188   -113    -66       N  
ATOM   1301  CA  ALA A 164       1.265  30.550  35.427  1.00 24.74           C  
ANISOU 1301  CA  ALA A 164     3178   2941   3282   -184   -104    -57       C  
ATOM   1302  C   ALA A 164       0.278  30.377  34.279  1.00 25.96           C  
ANISOU 1302  C   ALA A 164     3344   3106   3415   -178    -95    -48       C  
ATOM   1303  O   ALA A 164       0.677  30.301  33.112  1.00 22.25           O  
ANISOU 1303  O   ALA A 164     2874   2639   2940   -172    -81    -37       O  
ATOM   1304  CB  ALA A 164       1.565  29.210  36.094  1.00 22.55           C  
ANISOU 1304  CB  ALA A 164     2904   2669   2994   -182   -112    -64       C  
ATOM   1305  N   LEU A 165      -1.019  30.310  34.592  1.00 22.53           N  
ANISOU 1305  N   LEU A 165     2916   2681   2964   -179   -104    -53       N  
ATOM   1306  CA  LEU A 165      -2.033  30.221  33.543  1.00 24.14           C  
ANISOU 1306  CA  LEU A 165     3125   2902   3147   -173   -100    -49       C  
ATOM   1307  C   LEU A 165      -2.041  31.472  32.670  1.00 24.53           C  
ANISOU 1307  C   LEU A 165     3170   2950   3199   -161    -88    -29       C  
ATOM   1308  O   LEU A 165      -2.238  31.390  31.449  1.00 25.65           O  
ANISOU 1308  O   LEU A 165     3314   3109   3321   -150    -81    -19       O  
ATOM   1309  CB  LEU A 165      -3.404  29.969  34.176  1.00 23.79           C  
ANISOU 1309  CB  LEU A 165     3083   2866   3091   -177   -111    -60       C  
ATOM   1310  CG  LEU A 165      -3.580  28.514  34.618  1.00 27.57           C  
ANISOU 1310  CG  LEU A 165     3567   3346   3562   -186   -114    -75       C  
ATOM   1311  CD1 LEU A 165      -4.838  28.328  35.484  1.00 31.49           C  
ANISOU 1311  CD1 LEU A 165     4064   3846   4055   -191   -120    -84       C  
ATOM   1312  CD2 LEU A 165      -3.644  27.628  33.368  1.00 29.58           C  
ANISOU 1312  CD2 LEU A 165     3823   3613   3802   -186   -108    -82       C  
ATOM   1313  N   ALA A 166      -1.798  32.644  33.269  1.00 21.73           N  
ANISOU 1313  N   ALA A 166     2810   2577   2870   -162    -84    -23       N  
ATOM   1314  CA  ALA A 166      -1.793  33.865  32.475  1.00 25.48           C  
ANISOU 1314  CA  ALA A 166     3282   3044   3354   -149    -65      0       C  
ATOM   1315  C   ALA A 166      -0.656  33.880  31.456  1.00 26.96           C  
ANISOU 1315  C   ALA A 166     3469   3228   3549   -143    -46     16       C  
ATOM   1316  O   ALA A 166      -0.709  34.656  30.501  1.00 24.13           O  
ANISOU 1316  O   ALA A 166     3111   2868   3189   -126    -26     42       O  
ATOM   1317  CB  ALA A 166      -1.706  35.087  33.386  1.00 25.00           C  
ANISOU 1317  CB  ALA A 166     3215   2957   3327   -154    -60     -3       C  
ATOM   1318  N   CYS A 167       0.381  33.063  31.661  1.00 22.80           N  
ANISOU 1318  N   CYS A 167     2938   2695   3028   -153    -48      4       N  
ATOM   1319  CA  CYS A 167       1.479  32.904  30.720  1.00 23.45           C  
ANISOU 1319  CA  CYS A 167     3018   2775   3117   -148    -28     17       C  
ATOM   1320  C   CYS A 167       1.226  31.752  29.750  1.00 24.20           C  
ANISOU 1320  C   CYS A 167     3124   2897   3175   -140    -30     16       C  
ATOM   1321  O   CYS A 167       1.427  31.887  28.536  1.00 25.46           O  
ANISOU 1321  O   CYS A 167     3288   3066   3319   -124    -11     34       O  
ATOM   1322  CB  CYS A 167       2.781  32.659  31.503  1.00 24.80           C  
ANISOU 1322  CB  CYS A 167     3175   2928   3319   -162    -30      4       C  
ATOM   1323  SG  CYS A 167       4.238  32.525  30.473  1.00 26.88           S  
ANISOU 1323  SG  CYS A 167     3430   3183   3598   -157     -3     19       S  
ATOM   1324  N   ALA A 168       0.790  30.611  30.271  1.00 20.65           N  
ANISOU 1324  N   ALA A 168     2679   2457   2710   -149    -48     -7       N  
ATOM   1325  CA  ALA A 168       0.746  29.402  29.468  1.00 21.82           C  
ANISOU 1325  CA  ALA A 168     2835   2622   2832   -146    -47    -17       C  
ATOM   1326  C   ALA A 168      -0.531  29.290  28.638  1.00 27.32           C  
ANISOU 1326  C   ALA A 168     3538   3350   3492   -137    -53    -21       C  
ATOM   1327  O   ALA A 168      -0.535  28.604  27.615  1.00 24.60           O  
ANISOU 1327  O   ALA A 168     3200   3025   3122   -131    -48    -28       O  
ATOM   1328  CB  ALA A 168       0.884  28.169  30.372  1.00 22.46           C  
ANISOU 1328  CB  ALA A 168     2919   2697   2919   -159    -58    -38       C  
ATOM   1329  N   ALA A 169      -1.619  29.907  29.079  1.00 21.70           N  
ANISOU 1329  N   ALA A 169     2824   2644   2777   -136    -66    -20       N  
ATOM   1330  CA  ALA A 169      -2.900  29.703  28.405  1.00 20.45           C  
ANISOU 1330  CA  ALA A 169     2666   2520   2585   -129    -77    -28       C  
ATOM   1331  C   ALA A 169      -3.100  30.529  27.126  1.00 19.83           C  
ANISOU 1331  C   ALA A 169     2587   2467   2480   -102    -67     -4       C  
ATOM   1332  O   ALA A 169      -3.692  30.003  26.182  1.00 22.66           O  
ANISOU 1332  O   ALA A 169     2947   2862   2802    -93    -74    -15       O  
ATOM   1333  CB  ALA A 169      -4.052  29.943  29.390  1.00 25.08           C  
ANISOU 1333  CB  ALA A 169     3246   3106   3178   -137    -93    -37       C  
ATOM   1334  N   PRO A 170      -2.671  31.791  27.029  1.00 24.14           N  
ANISOU 1334  N   PRO A 170     3133   2997   3043    -88    -50     29       N  
ATOM   1335  CA  PRO A 170      -2.977  32.584  25.802  1.00 20.52           C  
ANISOU 1335  CA  PRO A 170     2676   2564   2555    -56    -37     60       C  
ATOM   1336  C   PRO A 170      -2.534  31.918  24.504  1.00 23.71           C  
ANISOU 1336  C   PRO A 170     3088   2998   2923    -42    -28     59       C  
ATOM   1337  O   PRO A 170      -3.280  31.967  23.515  1.00 22.39           O  
ANISOU 1337  O   PRO A 170     2921   2875   2710    -19    -33     65       O  
ATOM   1338  CB  PRO A 170      -2.239  33.912  26.041  1.00 21.83           C  
ANISOU 1338  CB  PRO A 170     2841   2692   2759    -49     -9     94       C  
ATOM   1339  CG  PRO A 170      -2.351  34.080  27.552  1.00 27.80           C  
ANISOU 1339  CG  PRO A 170     3591   3416   3554    -74    -22     75       C  
ATOM   1340  CD  PRO A 170      -2.156  32.668  28.104  1.00 24.17           C  
ANISOU 1340  CD  PRO A 170     3133   2961   3091    -98    -42     39       C  
ATOM   1341  N   PRO A 171      -1.359  31.271  24.444  1.00 23.03           N  
ANISOU 1341  N   PRO A 171     3007   2894   2851    -54    -14     51       N  
ATOM   1342  CA  PRO A 171      -0.953  30.620  23.175  1.00 24.97           C  
ANISOU 1342  CA  PRO A 171     3260   3168   3059    -40     -3     48       C  
ATOM   1343  C   PRO A 171      -1.838  29.457  22.766  1.00 21.59           C  
ANISOU 1343  C   PRO A 171     2833   2779   2591    -45    -27      7       C  
ATOM   1344  O   PRO A 171      -1.713  28.972  21.634  1.00 25.29           O  
ANISOU 1344  O   PRO A 171     3307   3280   3020    -31    -21     -1       O  
ATOM   1345  CB  PRO A 171       0.490  30.142  23.459  1.00 26.46           C  
ANISOU 1345  CB  PRO A 171     3451   3321   3281    -55     16     45       C  
ATOM   1346  CG  PRO A 171       0.972  31.037  24.558  1.00 29.46           C  
ANISOU 1346  CG  PRO A 171     3822   3658   3713    -67     21     61       C  
ATOM   1347  CD  PRO A 171      -0.240  31.318  25.414  1.00 24.35           C  
ANISOU 1347  CD  PRO A 171     3170   3014   3067    -75     -5     50       C  
ATOM   1348  N   LEU A 172      -2.688  28.940  23.659  1.00 22.53           N  
ANISOU 1348  N   LEU A 172     2944   2894   2721    -68    -52    -22       N  
ATOM   1349  CA  LEU A 172      -3.700  27.975  23.219  1.00 23.46           C  
ANISOU 1349  CA  LEU A 172     3057   3051   2805    -74    -74    -63       C  
ATOM   1350  C   LEU A 172      -4.849  28.623  22.461  1.00 22.07           C  
ANISOU 1350  C   LEU A 172     2872   2926   2587    -48    -89    -55       C  
ATOM   1351  O   LEU A 172      -5.547  27.920  21.717  1.00 24.71           O  
ANISOU 1351  O   LEU A 172     3201   3305   2884    -46   -106    -88       O  
ATOM   1352  CB  LEU A 172      -4.312  27.232  24.423  1.00 22.77           C  
ANISOU 1352  CB  LEU A 172     2962   2942   2747   -105    -90    -94       C  
ATOM   1353  CG  LEU A 172      -3.374  26.418  25.306  1.00 22.20           C  
ANISOU 1353  CG  LEU A 172     2898   2825   2714   -128    -79   -104       C  
ATOM   1354  CD1 LEU A 172      -4.166  25.826  26.506  1.00 29.08           C  
ANISOU 1354  CD1 LEU A 172     3762   3678   3609   -152    -92   -127       C  
ATOM   1355  CD2 LEU A 172      -2.718  25.314  24.496  1.00 24.37           C  
ANISOU 1355  CD2 LEU A 172     3180   3104   2975   -131    -66   -128       C  
ATOM   1356  N   VAL A 173      -5.105  29.923  22.672  1.00 21.21           N  
ANISOU 1356  N   VAL A 173     2760   2812   2486    -29    -85    -14       N  
ATOM   1357  CA  VAL A 173      -6.353  30.513  22.184  1.00 22.56           C  
ANISOU 1357  CA  VAL A 173     2919   3030   2623     -4   -103     -6       C  
ATOM   1358  C   VAL A 173      -6.122  31.777  21.361  1.00 31.41           C  
ANISOU 1358  C   VAL A 173     4046   4165   3722     40    -82     49       C  
ATOM   1359  O   VAL A 173      -7.024  32.610  21.209  1.00 29.00           O  
ANISOU 1359  O   VAL A 173     3731   3884   3402     66    -89     73       O  
ATOM   1360  CB  VAL A 173      -7.322  30.792  23.356  1.00 28.10           C  
ANISOU 1360  CB  VAL A 173     3608   3716   3354    -20   -120    -13       C  
ATOM   1361  CG1 VAL A 173      -7.794  29.479  23.947  1.00 25.49           C  
ANISOU 1361  CG1 VAL A 173     3268   3383   3034    -56   -138    -66       C  
ATOM   1362  CG2 VAL A 173      -6.666  31.650  24.431  1.00 23.90           C  
ANISOU 1362  CG2 VAL A 173     3083   3126   2873    -28   -101     16       C  
ATOM   1363  N   GLY A 174      -4.933  31.926  20.784  1.00 27.71           N  
ANISOU 1363  N   GLY A 174     3592   3682   3254     51    -52     73       N  
ATOM   1364  CA  GLY A 174      -4.758  32.918  19.744  1.00 29.77           C  
ANISOU 1364  CA  GLY A 174     3861   3965   3485     96    -28    124       C  
ATOM   1365  C   GLY A 174      -3.846  34.089  20.048  1.00 28.92           C  
ANISOU 1365  C   GLY A 174     3761   3804   3424    105     12    174       C  
ATOM   1366  O   GLY A 174      -3.773  34.993  19.221  1.00 25.62           O  
ANISOU 1366  O   GLY A 174     3350   3400   2986    145     37    223       O  
ATOM   1367  N   TRP A 175      -3.149  34.125  21.177  1.00 25.22           N  
ANISOU 1367  N   TRP A 175     3291   3275   3015     70     19    166       N  
ATOM   1368  CA  TRP A 175      -2.119  35.143  21.403  1.00 27.66           C  
ANISOU 1368  CA  TRP A 175     3604   3532   3373     73     59    205       C  
ATOM   1369  C   TRP A 175      -0.792  34.398  21.488  1.00 23.26           C  
ANISOU 1369  C   TRP A 175     3051   2949   2839     48     72    187       C  
ATOM   1370  O   TRP A 175      -0.558  33.681  22.465  1.00 24.02           O  
ANISOU 1370  O   TRP A 175     3141   3022   2962     13     53    150       O  
ATOM   1371  CB  TRP A 175      -2.382  35.936  22.681  1.00 29.82           C  
ANISOU 1371  CB  TRP A 175     3869   3760   3700     54     57    206       C  
ATOM   1372  CG  TRP A 175      -1.497  37.146  22.855  1.00 22.86           C  
ANISOU 1372  CG  TRP A 175     2988   2827   2871     58     99    244       C  
ATOM   1373  CD1 TRP A 175      -0.833  37.819  21.884  1.00 23.90           C  
ANISOU 1373  CD1 TRP A 175     3127   2952   3002     86    142    288       C  
ATOM   1374  CD2 TRP A 175      -1.215  37.829  24.081  1.00 23.65           C  
ANISOU 1374  CD2 TRP A 175     3080   2874   3034     32    105    236       C  
ATOM   1375  NE1 TRP A 175      -0.144  38.880  22.420  1.00 26.21           N  
ANISOU 1375  NE1 TRP A 175     3414   3185   3358     77    177    309       N  
ATOM   1376  CE2 TRP A 175      -0.360  38.903  23.774  1.00 25.59           C  
ANISOU 1376  CE2 TRP A 175     3326   3079   3320     43    153    274       C  
ATOM   1377  CE3 TRP A 175      -1.582  37.613  25.414  1.00 22.25           C  
ANISOU 1377  CE3 TRP A 175     2894   2678   2881      1     77    200       C  
ATOM   1378  CZ2 TRP A 175       0.137  39.772  24.748  1.00 27.67           C  
ANISOU 1378  CZ2 TRP A 175     3579   3286   3650     20    170    270       C  
ATOM   1379  CZ3 TRP A 175      -1.096  38.495  26.387  1.00 28.48           C  
ANISOU 1379  CZ3 TRP A 175     3676   3416   3730    -18     93    198       C  
ATOM   1380  CH2 TRP A 175      -0.245  39.545  26.048  1.00 24.81           C  
ANISOU 1380  CH2 TRP A 175     3209   2912   3307    -10    137    230       C  
ATOM   1381  N   SER A 176       0.059  34.575  20.475  1.00 22.39           N  
ANISOU 1381  N   SER A 176     2950   2843   2716     70    107    215       N  
ATOM   1382  CA  SER A 176       1.181  33.665  20.215  1.00 28.30           C  
ANISOU 1382  CA  SER A 176     3701   3583   3468     56    118    197       C  
ATOM   1383  C   SER A 176       0.636  32.266  19.930  1.00 31.50           C  
ANISOU 1383  C   SER A 176     4110   4030   3827     48     85    150       C  
ATOM   1384  O   SER A 176      -0.565  32.086  19.687  1.00 26.32           O  
ANISOU 1384  O   SER A 176     3452   3417   3129     58     57    135       O  
ATOM   1385  CB  SER A 176       2.188  33.628  21.381  1.00 23.89           C  
ANISOU 1385  CB  SER A 176     3132   2968   2978     19    123    183       C  
ATOM   1386  OG  SER A 176       3.404  32.951  21.007  1.00 26.06           O  
ANISOU 1386  OG  SER A 176     3408   3234   3262     13    143    177       O  
ATOM   1387  N   ARG A 177       1.507  31.264  19.953  1.00 20.58           N  
ANISOU 1387  N   ARG A 177     2729   2636   2454     29     89    124       N  
ATOM   1388  CA  ARG A 177       1.122  29.900  19.651  1.00 20.49           C  
ANISOU 1388  CA  ARG A 177     2723   2657   2408     19     66     76       C  
ATOM   1389  C   ARG A 177       2.284  29.014  20.081  1.00 23.78           C  
ANISOU 1389  C   ARG A 177     3138   3037   2859     -5     78     56       C  
ATOM   1390  O   ARG A 177       3.413  29.488  20.218  1.00 21.11           O  
ANISOU 1390  O   ARG A 177     2797   2666   2559     -5    106     82       O  
ATOM   1391  CB  ARG A 177       0.824  29.698  18.167  1.00 22.07           C  
ANISOU 1391  CB  ARG A 177     2934   2914   2539     52     73     78       C  
ATOM   1392  CG  ARG A 177       2.018  30.115  17.284  1.00 24.44           C  
ANISOU 1392  CG  ARG A 177     3243   3206   2835     77    118    116       C  
ATOM   1393  CD  ARG A 177       1.677  30.015  15.816  1.00 22.93           C  
ANISOU 1393  CD  ARG A 177     3065   3078   2569    116    125    121       C  
ATOM   1394  NE  ARG A 177       2.783  30.439  14.960  1.00 22.16           N  
ANISOU 1394  NE  ARG A 177     2979   2974   2466    143    174    162       N  
ATOM   1395  CZ  ARG A 177       2.769  30.298  13.645  1.00 30.47           C  
ANISOU 1395  CZ  ARG A 177     4046   4080   3453    180    189    170       C  
ATOM   1396  NH1 ARG A 177       1.716  29.793  13.022  1.00 29.91           N  
ANISOU 1396  NH1 ARG A 177     3977   4073   3313    194    156    137       N  
ATOM   1397  NH2 ARG A 177       3.848  30.629  12.942  1.00 24.60           N  
ANISOU 1397  NH2 ARG A 177     3312   3324   2709    202    238    208       N  
ATOM   1398  N   TYR A 178       1.998  27.737  20.281  1.00 20.70           N  
ANISOU 1398  N   TYR A 178     2750   2655   2460    -24     59     10       N  
ATOM   1399  CA  TYR A 178       3.047  26.755  20.513  1.00 21.58           C  
ANISOU 1399  CA  TYR A 178     2863   2739   2599    -40     72     -8       C  
ATOM   1400  C   TYR A 178       3.486  26.190  19.169  1.00 22.76           C  
ANISOU 1400  C   TYR A 178     3025   2917   2708    -21     94    -16       C  
ATOM   1401  O   TYR A 178       2.667  25.945  18.282  1.00 23.37           O  
ANISOU 1401  O   TYR A 178     3109   3040   2730     -7     84    -35       O  
ATOM   1402  CB  TYR A 178       2.569  25.637  21.462  1.00 19.54           C  
ANISOU 1402  CB  TYR A 178     2601   2466   2358    -69     48    -50       C  
ATOM   1403  CG  TYR A 178       2.358  26.141  22.874  1.00 20.97           C  
ANISOU 1403  CG  TYR A 178     2771   2617   2580    -86     31    -40       C  
ATOM   1404  CD1 TYR A 178       3.439  26.522  23.672  1.00 18.91           C  
ANISOU 1404  CD1 TYR A 178     2502   2319   2366    -93     42    -20       C  
ATOM   1405  CD2 TYR A 178       1.077  26.217  23.429  1.00 20.17           C  
ANISOU 1405  CD2 TYR A 178     2665   2527   2471    -96      4    -55       C  
ATOM   1406  CE1 TYR A 178       3.253  27.005  24.972  1.00 21.03           C  
ANISOU 1406  CE1 TYR A 178     2760   2564   2667   -107     26    -16       C  
ATOM   1407  CE2 TYR A 178       0.884  26.691  24.745  1.00 24.50           C  
ANISOU 1407  CE2 TYR A 178     3206   3049   3054   -110    -10    -47       C  
ATOM   1408  CZ  TYR A 178       1.972  27.087  25.504  1.00 22.74           C  
ANISOU 1408  CZ  TYR A 178     2977   2792   2873   -115      1    -28       C  
ATOM   1409  OH  TYR A 178       1.771  27.549  26.799  1.00 22.05           O  
ANISOU 1409  OH  TYR A 178     2881   2684   2813   -128    -14    -26       O  
ATOM   1410  N   ILE A 179       4.797  26.041  19.014  1.00 20.52           N  
ANISOU 1410  N   ILE A 179     2742   2607   2449    -18    126     -2       N  
ATOM   1411  CA  ILE A 179       5.420  25.698  17.741  1.00 23.90           C  
ANISOU 1411  CA  ILE A 179     3183   3058   2843      4    156     -1       C  
ATOM   1412  C   ILE A 179       6.608  24.779  18.025  1.00 21.68           C  
ANISOU 1412  C   ILE A 179     2898   2741   2599     -8    176    -14       C  
ATOM   1413  O   ILE A 179       7.293  24.954  19.054  1.00 20.52           O  
ANISOU 1413  O   ILE A 179     2736   2552   2507    -24    177     -1       O  
ATOM   1414  CB  ILE A 179       5.835  26.990  17.005  1.00 24.56           C  
ANISOU 1414  CB  ILE A 179     3268   3149   2915     34    186     53       C  
ATOM   1415  CG1 ILE A 179       6.298  26.738  15.577  1.00 24.52           C  
ANISOU 1415  CG1 ILE A 179     3278   3177   2861     65    218     58       C  
ATOM   1416  CG2 ILE A 179       6.939  27.700  17.786  1.00 23.10           C  
ANISOU 1416  CG2 ILE A 179     3067   2911   2797     24    208     86       C  
ATOM   1417  CD1 ILE A 179       6.431  28.052  14.747  1.00 27.24           C  
ANISOU 1417  CD1 ILE A 179     3629   3538   3184    102    249    116       C  
ATOM   1418  N   PRO A 180       6.884  23.772  17.181  1.00 22.29           N  
ANISOU 1418  N   PRO A 180     2988   2834   2648     -1    192    -43       N  
ATOM   1419  CA  PRO A 180       8.004  22.867  17.477  1.00 19.93           C  
ANISOU 1419  CA  PRO A 180     2686   2499   2388    -11    214    -54       C  
ATOM   1420  C   PRO A 180       9.349  23.589  17.440  1.00 22.62           C  
ANISOU 1420  C   PRO A 180     3015   2815   2765      1    248    -10       C  
ATOM   1421  O   PRO A 180       9.567  24.524  16.666  1.00 21.47           O  
ANISOU 1421  O   PRO A 180     2873   2685   2601     23    271     25       O  
ATOM   1422  CB  PRO A 180       7.905  21.802  16.374  1.00 20.76           C  
ANISOU 1422  CB  PRO A 180     2808   2632   2448     -1    227    -94       C  
ATOM   1423  CG  PRO A 180       6.431  21.786  16.020  1.00 24.11           C  
ANISOU 1423  CG  PRO A 180     3239   3100   2820     -3    194   -124       C  
ATOM   1424  CD  PRO A 180       6.015  23.236  16.112  1.00 20.31           C  
ANISOU 1424  CD  PRO A 180     2752   2634   2331     10    183    -78       C  
ATOM   1425  N   GLU A 181      10.276  23.106  18.264  1.00 20.87           N  
ANISOU 1425  N   GLU A 181     2779   2555   2597    -12    255    -10       N  
ATOM   1426  CA  GLU A 181      11.612  23.706  18.376  1.00 19.89           C  
ANISOU 1426  CA  GLU A 181     2636   2404   2518     -7    285     25       C  
ATOM   1427  C   GLU A 181      12.696  22.669  18.175  1.00 22.94           C  
ANISOU 1427  C   GLU A 181     3018   2773   2923     -2    313     14       C  
ATOM   1428  O   GLU A 181      12.490  21.473  18.429  1.00 20.72           O  
ANISOU 1428  O   GLU A 181     2745   2486   2640     -9    303    -21       O  
ATOM   1429  CB  GLU A 181      11.844  24.339  19.768  1.00 22.12           C  
ANISOU 1429  CB  GLU A 181     2893   2657   2856    -26    263     40       C  
ATOM   1430  CG  GLU A 181      10.736  25.253  20.237  1.00 23.82           C  
ANISOU 1430  CG  GLU A 181     3110   2881   3060    -34    233     46       C  
ATOM   1431  CD  GLU A 181      11.230  26.157  21.350  1.00 20.41           C  
ANISOU 1431  CD  GLU A 181     2651   2420   2683    -49    224     65       C  
ATOM   1432  OE1 GLU A 181      11.005  25.824  22.524  1.00 24.16           O  
ANISOU 1432  OE1 GLU A 181     3117   2883   3178    -66    193     48       O  
ATOM   1433  OE2 GLU A 181      11.860  27.178  21.013  1.00 20.30           O  
ANISOU 1433  OE2 GLU A 181     2626   2396   2691    -42    251     95       O  
ATOM   1434  N   GLY A 182      13.867  23.150  17.763  1.00 20.29           N  
ANISOU 1434  N   GLY A 182     2669   2426   2612     11    350     44       N  
ATOM   1435  CA  GLY A 182      15.059  22.288  17.744  1.00 22.33           C  
ANISOU 1435  CA  GLY A 182     2918   2664   2904     16    378     38       C  
ATOM   1436  C   GLY A 182      14.901  21.173  16.725  1.00 21.41           C  
ANISOU 1436  C   GLY A 182     2828   2565   2743     30    398      8       C  
ATOM   1437  O   GLY A 182      14.594  21.417  15.552  1.00 21.01           O  
ANISOU 1437  O   GLY A 182     2798   2546   2641     48    417     10       O  
ATOM   1438  N   MET A 183      15.101  19.916  17.183  1.00 20.68           N  
ANISOU 1438  N   MET A 183     2735   2453   2669     24    395    -21       N  
ATOM   1439  CA  MET A 183      14.865  18.756  16.313  1.00 22.00           C  
ANISOU 1439  CA  MET A 183     2929   2632   2799     32    413    -60       C  
ATOM   1440  C   MET A 183      13.360  18.463  16.088  1.00 22.58           C  
ANISOU 1440  C   MET A 183     3025   2733   2822     21    381    -99       C  
ATOM   1441  O   MET A 183      13.020  17.423  15.513  1.00 22.84           O  
ANISOU 1441  O   MET A 183     3076   2773   2828     21    390   -142       O  
ATOM   1442  CB  MET A 183      15.560  17.515  16.893  1.00 20.99           C  
ANISOU 1442  CB  MET A 183     2792   2468   2714     30    426    -77       C  
ATOM   1443  CG  MET A 183      17.087  17.560  16.688  1.00 21.22           C  
ANISOU 1443  CG  MET A 183     2801   2480   2782     48    467    -48       C  
ATOM   1444  SD  MET A 183      17.874  16.342  17.769  1.00 27.37           S  
ANISOU 1444  SD  MET A 183     3562   3216   3622     48    470    -54       S  
ATOM   1445  CE  MET A 183      17.069  14.871  17.124  1.00 21.40           C  
ANISOU 1445  CE  MET A 183     2844   2458   2831     47    483   -110       C  
ATOM   1446  N   GLN A 184      12.516  19.375  16.566  1.00 20.63           N  
ANISOU 1446  N   GLN A 184     2774   2500   2566     10    346    -85       N  
ATOM   1447  CA  GLN A 184      11.078  19.383  16.334  1.00 21.28           C  
ANISOU 1447  CA  GLN A 184     2871   2614   2600      2    315   -114       C  
ATOM   1448  C   GLN A 184      10.334  18.371  17.190  1.00 22.62           C  
ANISOU 1448  C   GLN A 184     3042   2765   2787    -22    288   -153       C  
ATOM   1449  O   GLN A 184       9.208  18.014  16.838  1.00 24.75           O  
ANISOU 1449  O   GLN A 184     3323   3060   3019    -31    269   -191       O  
ATOM   1450  CB  GLN A 184      10.757  19.151  14.848  1.00 21.07           C  
ANISOU 1450  CB  GLN A 184     2867   2631   2507     22    332   -138       C  
ATOM   1451  CG  GLN A 184      11.539  20.091  13.889  1.00 21.51           C  
ANISOU 1451  CG  GLN A 184     2925   2706   2542     52    368    -95       C  
ATOM   1452  CD  GLN A 184      11.144  21.551  14.086  1.00 24.30           C  
ANISOU 1452  CD  GLN A 184     3269   3071   2891     57    352    -49       C  
ATOM   1453  OE1 GLN A 184      10.047  21.953  13.695  1.00 22.87           O  
ANISOU 1453  OE1 GLN A 184     3098   2930   2660     63    328    -56       O  
ATOM   1454  NE2 GLN A 184      12.033  22.349  14.697  1.00 21.92           N  
ANISOU 1454  NE2 GLN A 184     2948   2737   2644     55    367     -4       N  
ATOM   1455  N   CYS A 185      10.920  17.912  18.314  1.00 20.17           N  
ANISOU 1455  N   CYS A 185     2718   2413   2534    -32    288   -144       N  
ATOM   1456  CA  CYS A 185      10.258  16.958  19.207  1.00 22.02           C  
ANISOU 1456  CA  CYS A 185     2955   2624   2789    -52    270   -174       C  
ATOM   1457  C   CYS A 185       9.822  17.569  20.537  1.00 21.45           C  
ANISOU 1457  C   CYS A 185     2867   2540   2742    -66    235   -151       C  
ATOM   1458  O   CYS A 185       9.339  16.842  21.409  1.00 22.03           O  
ANISOU 1458  O   CYS A 185     2942   2593   2837    -80    223   -167       O  
ATOM   1459  CB  CYS A 185      11.173  15.756  19.453  1.00 25.83           C  
ANISOU 1459  CB  CYS A 185     3436   3068   3309    -48    300   -182       C  
ATOM   1460  SG  CYS A 185      11.412  14.827  17.954  1.00 30.82           S  
ANISOU 1460  SG  CYS A 185     4089   3711   3909    -36    340   -224       S  
ATOM   1461  N   SER A 186       9.931  18.891  20.694  1.00 19.43           N  
ANISOU 1461  N   SER A 186     2600   2298   2485    -63    222   -116       N  
ATOM   1462  CA  SER A 186       9.335  19.615  21.808  1.00 19.84           C  
ANISOU 1462  CA  SER A 186     2640   2346   2552    -76    188   -101       C  
ATOM   1463  C   SER A 186       8.712  20.883  21.236  1.00 19.08           C  
ANISOU 1463  C   SER A 186     2546   2281   2422    -71    177    -86       C  
ATOM   1464  O   SER A 186       8.990  21.259  20.100  1.00 22.64           O  
ANISOU 1464  O   SER A 186     3004   2753   2846    -55    198    -77       O  
ATOM   1465  CB  SER A 186      10.352  19.957  22.918  1.00 23.55           C  
ANISOU 1465  CB  SER A 186     3088   2790   3071    -75    186    -71       C  
ATOM   1466  OG  SER A 186      11.283  20.951  22.479  1.00 23.77           O  
ANISOU 1466  OG  SER A 186     3102   2821   3109    -64    203    -41       O  
ATOM   1467  N   CYS A 187       7.793  21.498  21.980  1.00 18.82           N  
ANISOU 1467  N   CYS A 187     2509   2253   2390    -83    146    -82       N  
ATOM   1468  CA  CYS A 187       7.188  22.746  21.523  1.00 18.83           C  
ANISOU 1468  CA  CYS A 187     2511   2281   2364    -76    136    -63       C  
ATOM   1469  C   CYS A 187       7.412  23.851  22.542  1.00 20.21           C  
ANISOU 1469  C   CYS A 187     2668   2436   2574    -82    124    -33       C  
ATOM   1470  O   CYS A 187       7.482  23.594  23.744  1.00 21.36           O  
ANISOU 1470  O   CYS A 187     2804   2560   2751    -96    108    -37       O  
ATOM   1471  CB  CYS A 187       5.693  22.585  21.267  1.00 21.18           C  
ANISOU 1471  CB  CYS A 187     2818   2608   2622    -82    112    -90       C  
ATOM   1472  SG  CYS A 187       5.465  21.749  19.695  1.00 21.70           S  
ANISOU 1472  SG  CYS A 187     2901   2710   2633    -69    128   -124       S  
ATOM   1473  N   GLY A 188       7.527  25.078  22.049  1.00 18.69           N  
ANISOU 1473  N   GLY A 188     2472   2252   2376    -70    135     -3       N  
ATOM   1474  CA  GLY A 188       7.648  26.230  22.924  1.00 21.68           C  
ANISOU 1474  CA  GLY A 188     2836   2613   2790    -77    126     21       C  
ATOM   1475  C   GLY A 188       6.877  27.400  22.339  1.00 22.24           C  
ANISOU 1475  C   GLY A 188     2912   2703   2836    -65    127     43       C  
ATOM   1476  O   GLY A 188       6.154  27.238  21.354  1.00 20.81           O  
ANISOU 1476  O   GLY A 188     2746   2555   2606    -50    128     38       O  
ATOM   1477  N   ILE A 189       7.033  28.579  22.939  1.00 21.42           N  
ANISOU 1477  N   ILE A 189     2795   2579   2766    -69    129     66       N  
ATOM   1478  CA  ILE A 189       6.406  29.789  22.421  1.00 23.61           C  
ANISOU 1478  CA  ILE A 189     3077   2867   3028    -53    137     94       C  
ATOM   1479  C   ILE A 189       7.034  30.168  21.082  1.00 24.96           C  
ANISOU 1479  C   ILE A 189     3254   3047   3181    -27    179    125       C  
ATOM   1480  O   ILE A 189       8.226  29.948  20.845  1.00 23.36           O  
ANISOU 1480  O   ILE A 189     3045   2828   3003    -27    206    131       O  
ATOM   1481  CB  ILE A 189       6.577  30.918  23.452  1.00 21.38           C  
ANISOU 1481  CB  ILE A 189     2776   2551   2795    -67    135    107       C  
ATOM   1482  CG1 ILE A 189       5.873  30.557  24.743  1.00 25.55           C  
ANISOU 1482  CG1 ILE A 189     3301   3075   3332    -88     95     79       C  
ATOM   1483  CG2 ILE A 189       6.109  32.283  22.897  1.00 26.84           C  
ANISOU 1483  CG2 ILE A 189     3473   3243   3483    -48    155    144       C  
ATOM   1484  CD1 ILE A 189       4.406  30.330  24.565  1.00 29.66           C  
ANISOU 1484  CD1 ILE A 189     3835   3626   3808    -83     72     68       C  
ATOM   1485  N   ASP A 190       6.240  30.759  20.191  1.00 22.52           N  
ANISOU 1485  N   ASP A 190     2960   2768   2830     -2    186    146       N  
ATOM   1486  CA  ASP A 190       6.784  31.088  18.866  1.00 25.39           C  
ANISOU 1486  CA  ASP A 190     3333   3147   3169     29    228    179       C  
ATOM   1487  C   ASP A 190       7.696  32.324  18.966  1.00 25.97           C  
ANISOU 1487  C   ASP A 190     3393   3178   3296     31    269    221       C  
ATOM   1488  O   ASP A 190       7.246  33.458  18.806  1.00 23.67           O  
ANISOU 1488  O   ASP A 190     3104   2883   3008     47    283    255       O  
ATOM   1489  CB  ASP A 190       5.650  31.311  17.869  1.00 23.91           C  
ANISOU 1489  CB  ASP A 190     3163   3010   2912     61    221    191       C  
ATOM   1490  CG  ASP A 190       6.148  31.529  16.458  1.00 25.61           C  
ANISOU 1490  CG  ASP A 190     3393   3250   3089     98    264    224       C  
ATOM   1491  OD1 ASP A 190       7.389  31.655  16.254  1.00 24.11           O  
ANISOU 1491  OD1 ASP A 190     3198   3030   2933     98    304    243       O  
ATOM   1492  OD2 ASP A 190       5.299  31.540  15.544  1.00 26.93           O  
ANISOU 1492  OD2 ASP A 190     3574   3469   3188    129    257    229       O  
ATOM   1493  N   TYR A 191       9.009  32.092  19.185  1.00 23.54           N  
ANISOU 1493  N   TYR A 191     3070   2839   3035     17    292    219       N  
ATOM   1494  CA  TYR A 191      10.051  33.125  19.058  1.00 20.58           C  
ANISOU 1494  CA  TYR A 191     2680   2426   2715     19    339    256       C  
ATOM   1495  C   TYR A 191      10.491  33.329  17.618  1.00 25.13           C  
ANISOU 1495  C   TYR A 191     3270   3017   3260     54    390    294       C  
ATOM   1496  O   TYR A 191      11.292  34.233  17.351  1.00 26.25           O  
ANISOU 1496  O   TYR A 191     3400   3127   3445     60    439    331       O  
ATOM   1497  CB  TYR A 191      11.325  32.766  19.885  1.00 24.42           C  
ANISOU 1497  CB  TYR A 191     3136   2876   3265    -11    342    235       C  
ATOM   1498  CG  TYR A 191      11.006  32.016  21.144  1.00 22.69           C  
ANISOU 1498  CG  TYR A 191     2908   2657   3055    -38    289    191       C  
ATOM   1499  CD1 TYR A 191      10.341  32.646  22.184  1.00 20.10           C  
ANISOU 1499  CD1 TYR A 191     2573   2316   2748    -56    260    182       C  
ATOM   1500  CD2 TYR A 191      11.310  30.663  21.272  1.00 23.89           C  
ANISOU 1500  CD2 TYR A 191     3062   2822   3193    -44    272    161       C  
ATOM   1501  CE1 TYR A 191      10.020  31.971  23.332  1.00 21.63           C  
ANISOU 1501  CE1 TYR A 191     2761   2512   2947    -77    215    145       C  
ATOM   1502  CE2 TYR A 191      10.978  29.965  22.409  1.00 21.13           C  
ANISOU 1502  CE2 TYR A 191     2707   2471   2850    -64    228    127       C  
ATOM   1503  CZ  TYR A 191      10.317  30.629  23.438  1.00 24.28           C  
ANISOU 1503  CZ  TYR A 191     3099   2860   3266    -80    200    121       C  
ATOM   1504  OH  TYR A 191       9.952  29.957  24.572  1.00 24.09           O  
ANISOU 1504  OH  TYR A 191     3072   2838   3245    -97    160     91       O  
ATOM   1505  N   TYR A 192       9.983  32.524  16.688  1.00 24.02           N  
ANISOU 1505  N   TYR A 192     3154   2926   3047     78    383    286       N  
ATOM   1506  CA  TYR A 192      10.608  32.335  15.377  1.00 24.51           C  
ANISOU 1506  CA  TYR A 192     3229   3008   3074    109    428    310       C  
ATOM   1507  C   TYR A 192      10.018  33.180  14.267  1.00 26.09           C  
ANISOU 1507  C   TYR A 192     3451   3240   3224    154    457    357       C  
ATOM   1508  O   TYR A 192      10.744  33.547  13.337  1.00 26.50           O  
ANISOU 1508  O   TYR A 192     3509   3290   3270    181    511    397       O  
ATOM   1509  CB  TYR A 192      10.498  30.868  14.956  1.00 22.06           C  
ANISOU 1509  CB  TYR A 192     2933   2735   2713    111    406    266       C  
ATOM   1510  CG  TYR A 192      11.162  29.973  15.958  1.00 24.90           C  
ANISOU 1510  CG  TYR A 192     3274   3064   3122     74    386    226       C  
ATOM   1511  CD1 TYR A 192      10.454  29.475  17.038  1.00 24.18           C  
ANISOU 1511  CD1 TYR A 192     3178   2971   3040     47    334    188       C  
ATOM   1512  CD2 TYR A 192      12.508  29.652  15.842  1.00 23.25           C  
ANISOU 1512  CD2 TYR A 192     3051   2830   2952     71    421    230       C  
ATOM   1513  CE1 TYR A 192      11.061  28.662  17.984  1.00 29.91           C  
ANISOU 1513  CE1 TYR A 192     3887   3670   3808     20    317    158       C  
ATOM   1514  CE2 TYR A 192      13.129  28.855  16.806  1.00 22.71           C  
ANISOU 1514  CE2 TYR A 192     2963   2737   2929     42    401    198       C  
ATOM   1515  CZ  TYR A 192      12.402  28.357  17.843  1.00 23.91           C  
ANISOU 1515  CZ  TYR A 192     3113   2888   3084     19    350    164       C  
ATOM   1516  OH  TYR A 192      13.005  27.574  18.771  1.00 24.67           O  
ANISOU 1516  OH  TYR A 192     3191   2963   3220     -2    333    138       O  
ATOM   1517  N   THR A 193       8.719  33.447  14.306  1.00 26.77           N  
ANISOU 1517  N   THR A 193     3547   3357   3268    166    422    356       N  
ATOM   1518  CA  THR A 193       8.072  34.107  13.188  1.00 27.32           C  
ANISOU 1518  CA  THR A 193     3637   3468   3275    215    444    400       C  
ATOM   1519  C   THR A 193       7.277  35.294  13.701  1.00 27.35           C  
ANISOU 1519  C   THR A 193     3636   3455   3301    220    438    431       C  
ATOM   1520  O   THR A 193       6.853  35.312  14.860  1.00 29.07           O  
ANISOU 1520  O   THR A 193     3840   3649   3558    186    400    401       O  
ATOM   1521  CB  THR A 193       7.117  33.161  12.434  1.00 33.96           C  
ANISOU 1521  CB  THR A 193     4497   4384   4022    237    406    367       C  
ATOM   1522  OG1 THR A 193       5.903  33.001  13.180  1.00 30.20           O  
ANISOU 1522  OG1 THR A 193     4015   3924   3537    219    348    334       O  
ATOM   1523  CG2 THR A 193       7.763  31.799  12.198  1.00 31.80           C  
ANISOU 1523  CG2 THR A 193     4226   4120   3734    221    401    319       C  
ATOM   1524  N   PRO A 194       7.075  36.309  12.863  1.00 32.88           N  
ANISOU 1524  N   PRO A 194     4349   4166   3978    266    479    492       N  
ATOM   1525  CA  PRO A 194       6.228  37.431  13.298  1.00 34.82           C  
ANISOU 1525  CA  PRO A 194     4591   4396   4242    276    476    523       C  
ATOM   1526  C   PRO A 194       4.760  37.049  13.443  1.00 35.18           C  
ANISOU 1526  C   PRO A 194     4640   4497   4228    283    413    493       C  
ATOM   1527  O   PRO A 194       4.090  37.553  14.352  1.00 44.57           O  
ANISOU 1527  O   PRO A 194     5820   5664   5452    266    389    487       O  
ATOM   1528  CB  PRO A 194       6.445  38.480  12.198  1.00 42.21           C  
ANISOU 1528  CB  PRO A 194     5542   5335   5161    331    543    601       C  
ATOM   1529  CG  PRO A 194       7.630  38.002  11.386  1.00 42.90           C  
ANISOU 1529  CG  PRO A 194     5637   5424   5241    340    587    610       C  
ATOM   1530  CD  PRO A 194       7.661  36.521  11.528  1.00 37.63           C  
ANISOU 1530  CD  PRO A 194     4967   4789   4539    312    536    540       C  
ATOM   1531  N   HIS A 195       4.225  36.249  12.516  1.00 38.98           N  
ANISOU 1531  N   HIS A 195     5137   5052   4623    311    390    476       N  
ATOM   1532  CA  HIS A 195       2.864  35.711  12.530  1.00 33.82           C  
ANISOU 1532  CA  HIS A 195     4483   4459   3909    316    329    438       C  
ATOM   1533  C   HIS A 195       1.816  36.663  13.111  1.00 32.48           C  
ANISOU 1533  C   HIS A 195     4304   4282   3754    324    312    461       C  
ATOM   1534  O   HIS A 195       1.341  36.461  14.233  1.00 33.30           O  
ANISOU 1534  O   HIS A 195     4394   4363   3897    285    274    423       O  
ATOM   1535  CB  HIS A 195       2.774  34.368  13.230  1.00 33.76           C  
ANISOU 1535  CB  HIS A 195     4466   4454   3908    267    279    361       C  
ATOM   1536  CG  HIS A 195       1.594  33.572  12.765  1.00 35.62           C  
ANISOU 1536  CG  HIS A 195     4703   4764   4066    278    229    319       C  
ATOM   1537  ND1 HIS A 195       0.496  33.328  13.561  1.00 35.69           N  
ANISOU 1537  ND1 HIS A 195     4698   4783   4080    255    178    282       N  
ATOM   1538  CD2 HIS A 195       1.304  33.047  11.551  1.00 38.06           C  
ANISOU 1538  CD2 HIS A 195     5024   5145   4291    313    224    308       C  
ATOM   1539  CE1 HIS A 195      -0.397  32.637  12.874  1.00 40.11           C  
ANISOU 1539  CE1 HIS A 195     5258   5415   4567    271    142    246       C  
ATOM   1540  NE2 HIS A 195       0.069  32.455  11.652  1.00 38.52           N  
ANISOU 1540  NE2 HIS A 195     5073   5254   4309    306    167    260       N  
ATOM   1541  N   GLU A 196       1.525  37.749  12.388  1.00 32.19           N  
ANISOU 1541  N   GLU A 196     4277   4260   3694    378    347    528       N  
ATOM   1542  CA  GLU A 196       0.702  38.845  12.915  1.00 35.91           C  
ANISOU 1542  CA  GLU A 196     4740   4712   4192    391    347    562       C  
ATOM   1543  C   GLU A 196      -0.681  38.393  13.376  1.00 31.86           C  
ANISOU 1543  C   GLU A 196     4216   4245   3646    382    279    518       C  
ATOM   1544  O   GLU A 196      -1.270  39.025  14.262  1.00 39.54           O  
ANISOU 1544  O   GLU A 196     5177   5185   4662    370    268    522       O  
ATOM   1545  CB  GLU A 196       0.537  39.933  11.849  1.00 45.75           C  
ANISOU 1545  CB  GLU A 196     6001   5980   5402    461    396    644       C  
ATOM   1546  CG  GLU A 196       1.700  40.900  11.734  1.00 63.54           C  
ANISOU 1546  CG  GLU A 196     8261   8161   7721    468    475    703       C  
ATOM   1547  CD  GLU A 196       2.794  40.401  10.818  1.00 66.86           C  
ANISOU 1547  CD  GLU A 196     8694   8593   8116    479    513    713       C  
ATOM   1548  OE1 GLU A 196       2.631  39.303  10.232  1.00 67.06           O  
ANISOU 1548  OE1 GLU A 196     8726   8684   8069    484    477    673       O  
ATOM   1549  OE2 GLU A 196       3.817  41.113  10.685  1.00 73.45           O  
ANISOU 1549  OE2 GLU A 196     9532   9369   9008    482    580    759       O  
ATOM   1550  N   GLU A 197      -1.227  37.340  12.771  1.00 33.16           N  
ANISOU 1550  N   GLU A 197     4380   4483   3734    390    237    475       N  
ATOM   1551  CA  GLU A 197      -2.556  36.879  13.145  1.00 36.24           C  
ANISOU 1551  CA  GLU A 197     4755   4918   4095    381    175    430       C  
ATOM   1552  C   GLU A 197      -2.638  36.553  14.631  1.00 34.05           C  
ANISOU 1552  C   GLU A 197     4463   4584   3889    318    148    384       C  
ATOM   1553  O   GLU A 197      -3.682  36.757  15.263  1.00 31.85           O  
ANISOU 1553  O   GLU A 197     4170   4313   3619    312    116    371       O  
ATOM   1554  CB  GLU A 197      -2.926  35.655  12.315  1.00 36.14           C  
ANISOU 1554  CB  GLU A 197     4744   4986   4003    386    137    378       C  
ATOM   1555  CG  GLU A 197      -4.354  35.195  12.533  1.00 62.50           C  
ANISOU 1555  CG  GLU A 197     8062   8380   7306    381     76    332       C  
ATOM   1556  CD  GLU A 197      -4.677  33.960  11.730  1.00 74.86           C  
ANISOU 1556  CD  GLU A 197     9624  10019   8799    381     40    271       C  
ATOM   1557  OE1 GLU A 197      -3.726  33.242  11.353  1.00 70.75           O  
ANISOU 1557  OE1 GLU A 197     9119   9490   8274    367     58    250       O  
ATOM   1558  OE2 GLU A 197      -5.874  33.710  11.473  1.00 84.78           O  
ANISOU 1558  OE2 GLU A 197    10863  11344  10006    395     -5    242       O  
ATOM   1559  N   THR A 198      -1.552  36.047  15.215  1.00 30.69           N  
ANISOU 1559  N   THR A 198     4040   4105   3517    274    161    358       N  
ATOM   1560  CA  THR A 198      -1.551  35.738  16.643  1.00 29.86           C  
ANISOU 1560  CA  THR A 198     3921   3948   3476    219    137    317       C  
ATOM   1561  C   THR A 198      -0.754  36.753  17.466  1.00 30.74           C  
ANISOU 1561  C   THR A 198     4031   3982   3669    203    175    349       C  
ATOM   1562  O   THR A 198      -0.475  36.497  18.644  1.00 25.47           O  
ANISOU 1562  O   THR A 198     3353   3270   3056    158    160    316       O  
ATOM   1563  CB  THR A 198      -1.025  34.313  16.880  1.00 28.21           C  
ANISOU 1563  CB  THR A 198     3712   3738   3268    179    116    257       C  
ATOM   1564  OG1 THR A 198       0.211  34.139  16.200  1.00 31.94           O  
ANISOU 1564  OG1 THR A 198     4196   4199   3741    186    155    273       O  
ATOM   1565  CG2 THR A 198      -2.032  33.281  16.346  1.00 25.90           C  
ANISOU 1565  CG2 THR A 198     3417   3516   2909    183     72    210       C  
ATOM   1566  N   ASN A 199      -0.395  37.899  16.878  1.00 28.54           N  
ANISOU 1566  N   ASN A 199     3760   3686   3400    239    224    412       N  
ATOM   1567  CA  ASN A 199       0.258  38.990  17.599  1.00 32.34           C  
ANISOU 1567  CA  ASN A 199     4235   4092   3961    225    264    441       C  
ATOM   1568  C   ASN A 199       1.470  38.508  18.405  1.00 33.50           C  
ANISOU 1568  C   ASN A 199     4373   4186   4169    174    268    406       C  
ATOM   1569  O   ASN A 199       1.590  38.742  19.617  1.00 27.21           O  
ANISOU 1569  O   ASN A 199     3564   3344   3432    137    258    382       O  
ATOM   1570  CB  ASN A 199      -0.755  39.708  18.474  1.00 31.04           C  
ANISOU 1570  CB  ASN A 199     4060   3910   3821    221    245    442       C  
ATOM   1571  CG  ASN A 199      -1.816  40.386  17.649  1.00 41.22           C  
ANISOU 1571  CG  ASN A 199     5356   5245   5059    278    250    488       C  
ATOM   1572  OD1 ASN A 199      -1.546  41.384  17.002  1.00 42.56           O  
ANISOU 1572  OD1 ASN A 199     5535   5401   5237    317    301    550       O  
ATOM   1573  ND2 ASN A 199      -3.011  39.822  17.627  1.00 42.79           N  
ANISOU 1573  ND2 ASN A 199     5549   5503   5207    285    199    460       N  
ATOM   1574  N   ASN A 200       2.387  37.834  17.698  1.00 28.01           N  
ANISOU 1574  N   ASN A 200     3684   3502   3456    176    286    403       N  
ATOM   1575  CA  ASN A 200       3.466  37.086  18.344  1.00 25.82           C  
ANISOU 1575  CA  ASN A 200     3397   3192   3222    132    282    364       C  
ATOM   1576  C   ASN A 200       4.391  38.003  19.132  1.00 28.61           C  
ANISOU 1576  C   ASN A 200     3734   3473   3661    108    316    378       C  
ATOM   1577  O   ASN A 200       4.795  37.685  20.260  1.00 25.40           O  
ANISOU 1577  O   ASN A 200     3312   3037   3302     66    294    338       O  
ATOM   1578  CB  ASN A 200       4.283  36.325  17.287  1.00 32.20           C  
ANISOU 1578  CB  ASN A 200     4216   4025   3995    147    303    367       C  
ATOM   1579  CG  ASN A 200       3.729  34.948  16.959  1.00 33.68           C  
ANISOU 1579  CG  ASN A 200     4410   4268   4118    144    260    320       C  
ATOM   1580  OD1 ASN A 200       2.629  34.589  17.365  1.00 29.04           O  
ANISOU 1580  OD1 ASN A 200     3821   3708   3506    137    215    291       O  
ATOM   1581  ND2 ASN A 200       4.496  34.172  16.174  1.00 26.14           N  
ANISOU 1581  ND2 ASN A 200     3464   3330   3138    151    277    312       N  
ATOM   1582  N   GLU A 201       4.779  39.128  18.530  1.00 27.09           N  
ANISOU 1582  N   GLU A 201     3546   3256   3493    134    372    432       N  
ATOM   1583  CA  GLU A 201       5.794  39.979  19.142  1.00 32.92           C  
ANISOU 1583  CA  GLU A 201     4265   3924   4319    108    411    441       C  
ATOM   1584  C   GLU A 201       5.345  40.475  20.504  1.00 29.75           C  
ANISOU 1584  C   GLU A 201     3849   3487   3967     76    385    412       C  
ATOM   1585  O   GLU A 201       6.118  40.442  21.471  1.00 28.26           O  
ANISOU 1585  O   GLU A 201     3640   3260   3838     35    379    378       O  
ATOM   1586  CB  GLU A 201       6.124  41.174  18.238  1.00 31.61           C  
ANISOU 1586  CB  GLU A 201     4107   3732   4172    145    482    509       C  
ATOM   1587  CG  GLU A 201       7.200  42.082  18.832  1.00 42.47           C  
ANISOU 1587  CG  GLU A 201     5459   5030   5647    114    529    514       C  
ATOM   1588  CD  GLU A 201       7.550  43.273  17.951  1.00 54.44           C  
ANISOU 1588  CD  GLU A 201     6982   6512   7191    149    608    584       C  
ATOM   1589  OE1 GLU A 201       6.715  43.655  17.115  1.00 49.77           O  
ANISOU 1589  OE1 GLU A 201     6413   5952   6546    200    623    633       O  
ATOM   1590  OE2 GLU A 201       8.662  43.825  18.099  1.00 60.84           O  
ANISOU 1590  OE2 GLU A 201     7773   7265   8079    127    657    591       O  
ATOM   1591  N   SER A 202       4.091  40.911  20.615  1.00 25.55           N  
ANISOU 1591  N   SER A 202     3326   2973   3409     95    366    423       N  
ATOM   1592  CA  SER A 202       3.662  41.459  21.895  1.00 26.35           C  
ANISOU 1592  CA  SER A 202     3414   3038   3557     67    347    396       C  
ATOM   1593  C   SER A 202       3.604  40.380  22.969  1.00 27.02           C  
ANISOU 1593  C   SER A 202     3490   3137   3638     27    288    333       C  
ATOM   1594  O   SER A 202       3.853  40.661  24.142  1.00 28.37           O  
ANISOU 1594  O   SER A 202     3646   3272   3862     -7    277    302       O  
ATOM   1595  CB  SER A 202       2.303  42.165  21.766  1.00 31.63           C  
ANISOU 1595  CB  SER A 202     4094   3724   4200     99    343    424       C  
ATOM   1596  OG  SER A 202       1.286  41.283  21.353  1.00 29.49           O  
ANISOU 1596  OG  SER A 202     3834   3520   3851    119    298    413       O  
ATOM   1597  N   PHE A 203       3.267  39.147  22.603  1.00 25.04           N  
ANISOU 1597  N   PHE A 203     3249   2938   3327     31    253    313       N  
ATOM   1598  CA  PHE A 203       3.245  38.115  23.628  1.00 24.93           C  
ANISOU 1598  CA  PHE A 203     3227   2932   3314     -4    205    258       C  
ATOM   1599  C   PHE A 203       4.648  37.849  24.171  1.00 22.15           C  
ANISOU 1599  C   PHE A 203     2858   2546   3012    -35    214    237       C  
ATOM   1600  O   PHE A 203       4.826  37.668  25.376  1.00 24.79           O  
ANISOU 1600  O   PHE A 203     3178   2862   3377    -66    188    201       O  
ATOM   1601  CB  PHE A 203       2.643  36.804  23.105  1.00 23.52           C  
ANISOU 1601  CB  PHE A 203     3061   2809   3068      5    171    238       C  
ATOM   1602  CG  PHE A 203       2.647  35.725  24.153  1.00 21.82           C  
ANISOU 1602  CG  PHE A 203     2838   2595   2856    -29    130    188       C  
ATOM   1603  CD1 PHE A 203       1.596  35.625  25.055  1.00 22.92           C  
ANISOU 1603  CD1 PHE A 203     2977   2742   2991    -40     95    165       C  
ATOM   1604  CD2 PHE A 203       3.730  34.860  24.291  1.00 26.61           C  
ANISOU 1604  CD2 PHE A 203     3440   3194   3478    -47    130    168       C  
ATOM   1605  CE1 PHE A 203       1.600  34.679  26.057  1.00 26.02           C  
ANISOU 1605  CE1 PHE A 203     3364   3133   3389    -68     62    124       C  
ATOM   1606  CE2 PHE A 203       3.743  33.910  25.289  1.00 26.80           C  
ANISOU 1606  CE2 PHE A 203     3458   3217   3508    -73     96    128       C  
ATOM   1607  CZ  PHE A 203       2.679  33.811  26.182  1.00 27.12           C  
ANISOU 1607  CZ  PHE A 203     3499   3265   3541    -83     63    107       C  
ATOM   1608  N   VAL A 204       5.651  37.776  23.291  1.00 24.92           N  
ANISOU 1608  N   VAL A 204     3208   2892   3369    -25    250    259       N  
ATOM   1609  CA  VAL A 204       7.000  37.462  23.754  1.00 25.94           C  
ANISOU 1609  CA  VAL A 204     3317   2994   3546    -52    258    238       C  
ATOM   1610  C   VAL A 204       7.512  38.551  24.699  1.00 28.37           C  
ANISOU 1610  C   VAL A 204     3601   3251   3929    -78    273    230       C  
ATOM   1611  O   VAL A 204       8.135  38.263  25.729  1.00 24.91           O  
ANISOU 1611  O   VAL A 204     3141   2798   3525   -108    251    192       O  
ATOM   1612  CB  VAL A 204       7.928  37.232  22.543  1.00 25.23           C  
ANISOU 1612  CB  VAL A 204     3230   2909   3447    -34    300    266       C  
ATOM   1613  CG1 VAL A 204       9.367  37.027  22.991  1.00 27.77           C  
ANISOU 1613  CG1 VAL A 204     3525   3200   3826    -60    313    248       C  
ATOM   1614  CG2 VAL A 204       7.441  35.972  21.803  1.00 27.23           C  
ANISOU 1614  CG2 VAL A 204     3504   3215   3626    -15    276    257       C  
ATOM   1615  N  AILE A 205       7.256  39.815  24.365  0.49 28.00           N  
ANISOU 1615  N  AILE A 205     3556   3175   3907    -64    312    265       N  
ATOM   1616  N  BILE A 205       7.254  39.815  24.373  0.51 28.00           N  
ANISOU 1616  N  BILE A 205     3556   3175   3907    -64    312    264       N  
ATOM   1617  CA AILE A 205       7.636  40.907  25.258  0.49 29.63           C  
ANISOU 1617  CA AILE A 205     3741   3330   4189    -89    329    252       C  
ATOM   1618  CA BILE A 205       7.655  40.888  25.279  0.51 29.63           C  
ANISOU 1618  CA BILE A 205     3740   3329   4188    -90    328    251       C  
ATOM   1619  C  AILE A 205       6.912  40.773  26.589  0.49 25.59           C  
ANISOU 1619  C  AILE A 205     3225   2822   3675   -111    278    208       C  
ATOM   1620  C  BILE A 205       6.914  40.764  26.601  0.51 25.59           C  
ANISOU 1620  C  BILE A 205     3225   2823   3675   -112    277    207       C  
ATOM   1621  O  AILE A 205       7.521  40.893  27.659  0.49 26.38           O  
ANISOU 1621  O  AILE A 205     3302   2901   3821   -144    263    168       O  
ATOM   1622  O  BILE A 205       7.512  40.886  27.678  0.51 26.38           O  
ANISOU 1622  O  BILE A 205     3302   2901   3821   -144    262    167       O  
ATOM   1623  CB AILE A 205       7.352  42.268  24.595  0.49 31.18           C  
ANISOU 1623  CB AILE A 205     3945   3492   4411    -65    385    302       C  
ATOM   1624  CB BILE A 205       7.422  42.264  24.631  0.51 31.19           C  
ANISOU 1624  CB BILE A 205     3945   3492   4416    -67    385    300       C  
ATOM   1625  CG1AILE A 205       8.162  42.409  23.303  0.49 29.84           C  
ANISOU 1625  CG1AILE A 205     3779   3315   4244    -42    441    349       C  
ATOM   1626  CG1BILE A 205       8.215  42.379  23.331  0.51 29.84           C  
ANISOU 1626  CG1BILE A 205     3777   3314   4245    -44    440    347       C  
ATOM   1627  CG2AILE A 205       7.651  43.407  25.570  0.49 28.91           C  
ANISOU 1627  CG2AILE A 205     3634   3145   4204    -95    403    281       C  
ATOM   1628  CG2BILE A 205       7.810  43.377  25.601  0.51 28.91           C  
ANISOU 1628  CG2BILE A 205     3631   3143   4210    -99    404    278       C  
ATOM   1629  CD1AILE A 205       9.652  42.453  23.522  0.49 31.42           C  
ANISOU 1629  CD1AILE A 205     3948   3479   4510    -72    467    331       C  
ATOM   1630  CD1BILE A 205       8.028  43.704  22.661  0.51 33.95           C  
ANISOU 1630  CD1BILE A 205     4305   3798   4795    -16    504    402       C  
ATOM   1631  N   TYR A 206       5.605  40.491  26.540  1.00 24.90           N  
ANISOU 1631  N   TYR A 206     3160   2768   3533    -93    250    213       N  
ATOM   1632  CA  TYR A 206       4.829  40.282  27.759  1.00 24.22           C  
ANISOU 1632  CA  TYR A 206     3072   2690   3439   -110    204    174       C  
ATOM   1633  C   TYR A 206       5.396  39.139  28.589  1.00 31.76           C  
ANISOU 1633  C   TYR A 206     4017   3663   4389   -136    164    130       C  
ATOM   1634  O   TYR A 206       5.498  39.240  29.821  1.00 27.71           O  
ANISOU 1634  O   TYR A 206     3489   3138   3900   -160    140     93       O  
ATOM   1635  CB  TYR A 206       3.380  39.998  27.383  1.00 22.87           C  
ANISOU 1635  CB  TYR A 206     2924   2559   3208    -84    183    188       C  
ATOM   1636  CG  TYR A 206       2.553  39.242  28.402  1.00 23.53           C  
ANISOU 1636  CG  TYR A 206     3010   2666   3264    -98    132    150       C  
ATOM   1637  CD1 TYR A 206       2.084  39.866  29.573  1.00 23.45           C  
ANISOU 1637  CD1 TYR A 206     2994   2635   3282   -114    119    127       C  
ATOM   1638  CD2 TYR A 206       2.204  37.912  28.187  1.00 23.03           C  
ANISOU 1638  CD2 TYR A 206     2956   2646   3149    -96    100    136       C  
ATOM   1639  CE1 TYR A 206       1.286  39.167  30.485  1.00 22.56           C  
ANISOU 1639  CE1 TYR A 206     2885   2546   3142   -124     77     96       C  
ATOM   1640  CE2 TYR A 206       1.415  37.205  29.104  1.00 25.46           C  
ANISOU 1640  CE2 TYR A 206     3266   2972   3435   -108     60    105       C  
ATOM   1641  CZ  TYR A 206       0.951  37.834  30.241  1.00 26.91           C  
ANISOU 1641  CZ  TYR A 206     3444   3137   3644   -121     49     87       C  
ATOM   1642  OH  TYR A 206       0.142  37.108  31.117  1.00 28.26           O  
ANISOU 1642  OH  TYR A 206     3619   3327   3791   -130     14     60       O  
ATOM   1643  N   MET A 207       5.775  38.040  27.936  1.00 22.69           N  
ANISOU 1643  N   MET A 207     2874   2543   3205   -128    157    134       N  
ATOM   1644  CA  MET A 207       6.272  36.900  28.700  1.00 26.74           C  
ANISOU 1644  CA  MET A 207     3377   3071   3711   -147    122     98       C  
ATOM   1645  C   MET A 207       7.597  37.224  29.370  1.00 23.60           C  
ANISOU 1645  C   MET A 207     2949   2645   3372   -171    130     77       C  
ATOM   1646  O   MET A 207       7.791  36.940  30.558  1.00 27.26           O  
ANISOU 1646  O   MET A 207     3399   3112   3848   -190     97     42       O  
ATOM   1647  CB  MET A 207       6.431  35.667  27.798  1.00 25.33           C  
ANISOU 1647  CB  MET A 207     3211   2923   3488   -132    119    105       C  
ATOM   1648  CG  MET A 207       6.899  34.440  28.586  1.00 23.17           C  
ANISOU 1648  CG  MET A 207     2931   2663   3210   -147     87     72       C  
ATOM   1649  SD  MET A 207       7.049  32.984  27.501  1.00 29.87           S  
ANISOU 1649  SD  MET A 207     3796   3542   4012   -131     90     77       S  
ATOM   1650  CE  MET A 207       8.366  33.517  26.510  1.00 23.51           C  
ANISOU 1650  CE  MET A 207     2978   2717   3237   -123    138    105       C  
ATOM   1651  N   PHE A 208       8.532  37.822  28.631  1.00 20.76           N  
ANISOU 1651  N   PHE A 208     2577   2261   3051   -169    172     99       N  
ATOM   1652  CA  PHE A 208       9.832  38.074  29.253  1.00 21.45           C  
ANISOU 1652  CA  PHE A 208     2629   2325   3197   -194    178     74       C  
ATOM   1653  C   PHE A 208       9.762  39.147  30.329  1.00 31.76           C  
ANISOU 1653  C   PHE A 208     3916   3602   4550   -217    173     46       C  
ATOM   1654  O   PHE A 208      10.542  39.107  31.292  1.00 28.93           O  
ANISOU 1654  O   PHE A 208     3528   3240   4225   -241    153      7       O  
ATOM   1655  CB  PHE A 208      10.865  38.473  28.206  1.00 23.10           C  
ANISOU 1655  CB  PHE A 208     2825   2510   3440   -189    230    104       C  
ATOM   1656  CG  PHE A 208      11.537  37.299  27.578  1.00 32.29           C  
ANISOU 1656  CG  PHE A 208     3991   3700   4579   -178    230    110       C  
ATOM   1657  CD1 PHE A 208      12.509  36.585  28.277  1.00 37.51           C  
ANISOU 1657  CD1 PHE A 208     4624   4369   5259   -194    207     79       C  
ATOM   1658  CD2 PHE A 208      11.169  36.875  26.317  1.00 30.24           C  
ANISOU 1658  CD2 PHE A 208     3759   3460   4271   -149    251    145       C  
ATOM   1659  CE1 PHE A 208      13.126  35.481  27.703  1.00 33.37           C  
ANISOU 1659  CE1 PHE A 208     4102   3865   4713   -182    210     86       C  
ATOM   1660  CE2 PHE A 208      11.786  35.775  25.739  1.00 36.22           C  
ANISOU 1660  CE2 PHE A 208     4519   4239   5005   -140    253    147       C  
ATOM   1661  CZ  PHE A 208      12.760  35.077  26.440  1.00 29.22           C  
ANISOU 1661  CZ  PHE A 208     3606   3354   4144   -156    234    118       C  
ATOM   1662  N   VAL A 209       8.868  40.120  30.184  1.00 24.81           N  
ANISOU 1662  N   VAL A 209     3051   2702   3675   -210    192     63       N  
ATOM   1663  CA  VAL A 209       8.776  41.176  31.198  1.00 24.98           C  
ANISOU 1663  CA  VAL A 209     3056   2691   3744   -232    191     32       C  
ATOM   1664  C   VAL A 209       7.999  40.694  32.417  1.00 25.95           C  
ANISOU 1664  C   VAL A 209     3186   2842   3834   -239    138     -4       C  
ATOM   1665  O   VAL A 209       8.493  40.744  33.552  1.00 26.34           O  
ANISOU 1665  O   VAL A 209     3211   2890   3906   -263    112    -50       O  
ATOM   1666  CB  VAL A 209       8.151  42.448  30.598  1.00 27.35           C  
ANISOU 1666  CB  VAL A 209     3369   2954   4069   -219    238     67       C  
ATOM   1667  CG1 VAL A 209       7.839  43.448  31.711  1.00 29.23           C  
ANISOU 1667  CG1 VAL A 209     3596   3161   4351   -240    234     31       C  
ATOM   1668  CG2 VAL A 209       9.097  43.040  29.591  1.00 25.41           C  
ANISOU 1668  CG2 VAL A 209     3111   2673   3870   -215    297    100       C  
ATOM   1669  N   VAL A 210       6.774  40.217  32.204  1.00 23.23           N  
ANISOU 1669  N   VAL A 210     2872   2524   3432   -218    120     14       N  
ATOM   1670  CA  VAL A 210       5.897  39.869  33.322  1.00 23.98           C  
ANISOU 1670  CA  VAL A 210     2975   2639   3496   -223     78    -16       C  
ATOM   1671  C   VAL A 210       6.274  38.536  33.950  1.00 25.32           C  
ANISOU 1671  C   VAL A 210     3141   2845   3635   -228     37    -40       C  
ATOM   1672  O   VAL A 210       6.191  38.370  35.174  1.00 23.54           O  
ANISOU 1672  O   VAL A 210     2908   2631   3405   -240      5    -75       O  
ATOM   1673  CB  VAL A 210       4.429  39.873  32.862  1.00 24.57           C  
ANISOU 1673  CB  VAL A 210     3079   2728   3527   -199     77     12       C  
ATOM   1674  CG1 VAL A 210       3.536  39.326  33.959  1.00 30.98           C  
ANISOU 1674  CG1 VAL A 210     3900   3565   4306   -203     36    -16       C  
ATOM   1675  CG2 VAL A 210       4.033  41.300  32.478  1.00 30.61           C  
ANISOU 1675  CG2 VAL A 210     3846   3455   4328   -191    118     34       C  
ATOM   1676  N   HIS A 211       6.657  37.556  33.139  1.00 23.42           N  
ANISOU 1676  N   HIS A 211     2906   2623   3369   -216     39    -20       N  
ATOM   1677  CA  HIS A 211       6.847  36.200  33.642  1.00 19.69           C  
ANISOU 1677  CA  HIS A 211     2435   2182   2863   -216      5    -36       C  
ATOM   1678  C   HIS A 211       8.308  35.789  33.639  1.00 23.71           C  
ANISOU 1678  C   HIS A 211     2917   2691   3399   -223      8    -45       C  
ATOM   1679  O   HIS A 211       8.602  34.581  33.615  1.00 24.09           O  
ANISOU 1679  O   HIS A 211     2969   2762   3421   -215     -8    -44       O  
ATOM   1680  CB  HIS A 211       5.976  35.239  32.828  1.00 22.99           C  
ANISOU 1680  CB  HIS A 211     2881   2624   3229   -196      2    -13       C  
ATOM   1681  CG  HIS A 211       4.510  35.516  32.994  1.00 23.26           C  
ANISOU 1681  CG  HIS A 211     2935   2666   3236   -190     -8    -10       C  
ATOM   1682  ND1 HIS A 211       3.827  35.221  34.162  1.00 21.41           N  
ANISOU 1682  ND1 HIS A 211     2706   2443   2987   -196    -37    -33       N  
ATOM   1683  CD2 HIS A 211       3.617  36.146  32.184  1.00 28.73           C  
ANISOU 1683  CD2 HIS A 211     3642   3356   3917   -175     11     15       C  
ATOM   1684  CE1 HIS A 211       2.565  35.606  34.040  1.00 29.43           C  
ANISOU 1684  CE1 HIS A 211     3736   3462   3984   -187    -37    -24       C  
ATOM   1685  NE2 HIS A 211       2.407  36.163  32.846  1.00 24.97           N  
ANISOU 1685  NE2 HIS A 211     3177   2891   3421   -174    -10      5       N  
ATOM   1686  N   PHE A 212       9.230  36.741  33.472  1.00 25.52           N  
ANISOU 1686  N   PHE A 212     3121   2893   3682   -236     33    -48       N  
ATOM   1687  CA  PHE A 212      10.617  36.446  33.820  1.00 23.80           C  
ANISOU 1687  CA  PHE A 212     2869   2678   3496   -248     28    -68       C  
ATOM   1688  C   PHE A 212      11.337  37.554  34.593  1.00 27.35           C  
ANISOU 1688  C   PHE A 212     3281   3105   4005   -273     30   -102       C  
ATOM   1689  O   PHE A 212      11.821  37.333  35.710  1.00 26.91           O  
ANISOU 1689  O   PHE A 212     3202   3068   3954   -284     -4   -140       O  
ATOM   1690  CB  PHE A 212      11.329  36.108  32.514  1.00 21.87           C  
ANISOU 1690  CB  PHE A 212     2623   2427   3259   -237     63    -36       C  
ATOM   1691  CG  PHE A 212      12.808  35.841  32.649  1.00 29.00           C  
ANISOU 1691  CG  PHE A 212     3488   3331   4200   -246     65    -50       C  
ATOM   1692  CD1 PHE A 212      13.268  34.681  33.256  1.00 28.69           C  
ANISOU 1692  CD1 PHE A 212     3440   3323   4139   -240     32    -64       C  
ATOM   1693  CD2 PHE A 212      13.729  36.742  32.135  1.00 36.04           C  
ANISOU 1693  CD2 PHE A 212     4351   4191   5150   -259    105    -45       C  
ATOM   1694  CE1 PHE A 212      14.625  34.435  33.369  1.00 28.84           C  
ANISOU 1694  CE1 PHE A 212     3420   3345   4192   -245     34    -76       C  
ATOM   1695  CE2 PHE A 212      15.091  36.504  32.244  1.00 36.61           C  
ANISOU 1695  CE2 PHE A 212     4384   4266   5262   -268    108    -59       C  
ATOM   1696  CZ  PHE A 212      15.536  35.344  32.856  1.00 29.68           C  
ANISOU 1696  CZ  PHE A 212     3495   3423   4359   -260     70    -75       C  
ATOM   1697  N  AILE A 213      11.322  38.772  34.048  0.77 25.06           N  
ANISOU 1697  N  AILE A 213     2987   2775   3759   -282     71    -92       N  
ATOM   1698  N  BILE A 213      11.290  38.778  34.067  0.23 25.27           N  
ANISOU 1698  N  BILE A 213     3014   2802   3785   -282     70    -92       N  
ATOM   1699  CA AILE A 213      12.078  39.864  34.650  0.77 28.11           C  
ANISOU 1699  CA AILE A 213     3335   3133   4212   -310     81   -128       C  
ATOM   1700  CA BILE A 213      12.075  39.864  34.648  0.23 28.15           C  
ANISOU 1700  CA BILE A 213     3340   3137   4217   -310     81   -127       C  
ATOM   1701  C  AILE A 213      11.445  40.287  35.968  0.77 27.50           C  
ANISOU 1701  C  AILE A 213     3258   3063   4129   -322     47   -170       C  
ATOM   1702  C  BILE A 213      11.463  40.321  35.967  0.23 27.60           C  
ANISOU 1702  C  BILE A 213     3269   3074   4143   -323     48   -171       C  
ATOM   1703  O  AILE A 213      12.139  40.468  36.969  0.77 28.07           O  
ANISOU 1703  O  AILE A 213     3296   3144   4226   -342     22   -219       O  
ATOM   1704  O  BILE A 213      12.169  40.494  36.965  0.23 28.10           O  
ANISOU 1704  O  BILE A 213     3298   3146   4232   -343     23   -220       O  
ATOM   1705  CB AILE A 213      12.184  41.050  33.676  0.77 30.15           C  
ANISOU 1705  CB AILE A 213     3593   3340   4524   -314    143   -100       C  
ATOM   1706  CB BILE A 213      12.206  41.031  33.651  0.23 30.10           C  
ANISOU 1706  CB BILE A 213     3586   3334   4517   -314    143    -99       C  
ATOM   1707  CG1AILE A 213      13.168  40.729  32.552  0.77 29.97           C  
ANISOU 1707  CG1AILE A 213     3558   3310   4519   -307    179    -68       C  
ATOM   1708  CG1BILE A 213      13.143  40.652  32.498  0.23 29.98           C  
ANISOU 1708  CG1BILE A 213     3561   3313   4516   -305    178    -65       C  
ATOM   1709  CG2AILE A 213      12.565  42.327  34.415  0.77 30.68           C  
ANISOU 1709  CG2AILE A 213     3628   3370   4661   -345    156   -142       C  
ATOM   1710  CG2BILE A 213      12.683  42.292  34.360  0.23 30.55           C  
ANISOU 1710  CG2BILE A 213     3609   3353   4648   -346    158   -142       C  
ATOM   1711  CD1AILE A 213      13.457  41.912  31.688  0.77 39.05           C  
ANISOU 1711  CD1AILE A 213     4701   4408   5728   -311    244    -41       C  
ATOM   1712  CD1BILE A 213      14.553  40.302  32.930  0.23 30.36           C  
ANISOU 1712  CD1BILE A 213     3562   3371   4602   -324    166    -98       C  
ATOM   1713  N  AILE A 214      10.124  40.505  35.977  0.77 27.42           N  
ANISOU 1713  N  AILE A 214     3282   3049   4085   -310     47   -155       N  
ATOM   1714  N  BILE A 214      10.144  40.537  35.986  0.23 27.53           N  
ANISOU 1714  N  BILE A 214     3296   3062   4101   -310     47   -156       N  
ATOM   1715  CA AILE A 214       9.473  40.995  37.196  0.77 27.19           C  
ANISOU 1715  CA AILE A 214     3256   3024   4053   -320     21   -195       C  
ATOM   1716  CA BILE A 214       9.490  40.999  37.213  0.23 27.26           C  
ANISOU 1716  CA BILE A 214     3264   3033   4062   -320     21   -196       C  
ATOM   1717  C  AILE A 214       9.635  40.005  38.346  0.77 29.90           C  
ANISOU 1717  C  AILE A 214     3591   3415   4353   -318    -34   -227       C  
ATOM   1718  C  BILE A 214       9.652  39.999  38.353  0.23 29.79           C  
ANISOU 1718  C  BILE A 214     3577   3401   4340   -319    -34   -228       C  
ATOM   1719  O  AILE A 214      10.026  40.431  39.447  0.77 27.53           O  
ANISOU 1719  O  AILE A 214     3266   3122   4072   -336    -56   -277       O  
ATOM   1720  O  BILE A 214      10.033  40.417  39.459  0.23 27.59           O  
ANISOU 1720  O  BILE A 214     3273   3130   4078   -336    -57   -278       O  
ATOM   1721  CB AILE A 214       8.003  41.354  36.908  0.77 28.54           C  
ANISOU 1721  CB AILE A 214     3464   3183   4195   -303     33   -167       C  
ATOM   1722  CB BILE A 214       8.019  41.353  36.930  0.23 28.53           C  
ANISOU 1722  CB BILE A 214     3462   3182   4194   -304     33   -168       C  
ATOM   1723  CG1AILE A 214       7.911  42.726  36.225  0.77 28.14           C  
ANISOU 1723  CG1AILE A 214     3412   3078   4200   -308     87   -149       C  
ATOM   1724  CG1BILE A 214       7.934  42.652  36.127  0.23 28.15           C  
ANISOU 1724  CG1BILE A 214     3415   3082   4200   -306     88   -145       C  
ATOM   1725  CG2AILE A 214       7.173  41.283  38.192  0.77 28.49           C  
ANISOU 1725  CG2AILE A 214     3468   3198   4157   -305     -4   -201       C  
ATOM   1726  CG2BILE A 214       7.233  41.450  38.231  0.23 28.37           C  
ANISOU 1726  CG2BILE A 214     3451   3179   4151   -308     -1   -205       C  
ATOM   1727  CD1AILE A 214       6.482  43.148  35.897  0.77 32.67           C  
ANISOU 1727  CD1AILE A 214     4021   3644   4749   -287    102   -118       C  
ATOM   1728  CD1BILE A 214       8.621  43.819  36.790  0.23 31.02           C  
ANISOU 1728  CD1BILE A 214     3745   3406   4634   -337    105   -191       C  
ATOM   1729  N   PRO A 215       9.400  38.692  38.169  1.00 27.97           N  
ANISOU 1729  N   PRO A 215     3366   3206   4054   -297    -55   -203       N  
ATOM   1730  CA  PRO A 215       9.681  37.751  39.282  1.00 28.06           C  
ANISOU 1730  CA  PRO A 215     3369   3261   4030   -292   -101   -229       C  
ATOM   1731  C   PRO A 215      11.116  37.781  39.783  1.00 26.96           C  
ANISOU 1731  C   PRO A 215     3184   3135   3925   -305   -116   -263       C  
ATOM   1732  O   PRO A 215      11.350  37.754  40.998  1.00 25.26           O  
ANISOU 1732  O   PRO A 215     2951   2948   3699   -309   -152   -303       O  
ATOM   1733  CB  PRO A 215       9.338  36.376  38.675  1.00 28.31           C  
ANISOU 1733  CB  PRO A 215     3428   3315   4013   -268   -106   -189       C  
ATOM   1734  CG  PRO A 215       8.369  36.654  37.629  1.00 28.94           C  
ANISOU 1734  CG  PRO A 215     3539   3373   4085   -260    -76   -154       C  
ATOM   1735  CD  PRO A 215       8.702  38.017  37.060  1.00 24.49           C  
ANISOU 1735  CD  PRO A 215     2960   2768   3578   -275    -39   -153       C  
ATOM   1736  N   LEU A 216      12.101  37.861  38.887  1.00 28.28           N  
ANISOU 1736  N   LEU A 216     3329   3284   4133   -312    -89   -249       N  
ATOM   1737  CA  LEU A 216      13.484  37.870  39.359  1.00 25.25           C  
ANISOU 1737  CA  LEU A 216     2894   2915   3784   -324   -105   -283       C  
ATOM   1738  C   LEU A 216      13.787  39.143  40.143  1.00 28.18           C  
ANISOU 1738  C   LEU A 216     3233   3271   4205   -354   -108   -339       C  
ATOM   1739  O   LEU A 216      14.529  39.108  41.134  1.00 30.49           O  
ANISOU 1739  O   LEU A 216     3487   3595   4503   -363   -143   -386       O  
ATOM   1740  CB  LEU A 216      14.449  37.730  38.174  1.00 26.95           C  
ANISOU 1740  CB  LEU A 216     3091   3110   4037   -326    -69   -255       C  
ATOM   1741  CG  LEU A 216      14.476  36.328  37.557  1.00 33.05           C  
ANISOU 1741  CG  LEU A 216     3886   3907   4765   -297    -72   -214       C  
ATOM   1742  CD1 LEU A 216      15.519  36.291  36.452  1.00 42.61           C  
ANISOU 1742  CD1 LEU A 216     5075   5098   6016   -299    -34   -192       C  
ATOM   1743  CD2 LEU A 216      14.780  35.287  38.612  1.00 32.01           C  
ANISOU 1743  CD2 LEU A 216     3744   3824   4595   -282   -120   -231       C  
ATOM   1744  N   ILE A 217      13.188  40.267  39.737  1.00 36.25           N  
ANISOU 1744  N   ILE A 217     4268   4246   5261   -369    -71   -336       N  
ATOM   1745  CA  ILE A 217      13.353  41.515  40.484  1.00 28.59           C  
ANISOU 1745  CA  ILE A 217     3269   3252   4341   -399    -68   -392       C  
ATOM   1746  C   ILE A 217      12.848  41.348  41.911  1.00 28.00           C  
ANISOU 1746  C   ILE A 217     3200   3220   4221   -395   -119   -435       C  
ATOM   1747  O   ILE A 217      13.497  41.777  42.874  1.00 37.14           O  
ANISOU 1747  O   ILE A 217     4318   4394   5399   -415   -145   -497       O  
ATOM   1748  CB  ILE A 217      12.621  42.668  39.778  1.00 33.50           C  
ANISOU 1748  CB  ILE A 217     3913   3813   5002   -408    -15   -371       C  
ATOM   1749  CG1 ILE A 217      13.355  43.075  38.502  1.00 33.28           C  
ANISOU 1749  CG1 ILE A 217     3870   3741   5032   -415     40   -337       C  
ATOM   1750  CG2 ILE A 217      12.478  43.856  40.723  1.00 39.62           C  
ANISOU 1750  CG2 ILE A 217     4671   4566   5818   -435    -16   -431       C  
ATOM   1751  CD1 ILE A 217      12.584  44.127  37.677  1.00 38.34           C  
ANISOU 1751  CD1 ILE A 217     4539   4324   5705   -413     98   -302       C  
ATOM   1752  N   VAL A 218      11.668  40.756  42.071  1.00 25.83           N  
ANISOU 1752  N   VAL A 218     2970   2962   3881   -371   -132   -407       N  
ATOM   1753  CA  VAL A 218      11.135  40.565  43.414  1.00 31.23           C  
ANISOU 1753  CA  VAL A 218     3662   3685   4517   -364   -175   -443       C  
ATOM   1754  C   VAL A 218      12.049  39.647  44.226  1.00 30.85           C  
ANISOU 1754  C   VAL A 218     3586   3696   4439   -353   -223   -466       C  
ATOM   1755  O   VAL A 218      12.345  39.909  45.401  1.00 32.31           O  
ANISOU 1755  O   VAL A 218     3747   3914   4615   -359   -257   -521       O  
ATOM   1756  CB  VAL A 218       9.703  40.004  43.353  1.00 27.81           C  
ANISOU 1756  CB  VAL A 218     3283   3258   4025   -338   -176   -402       C  
ATOM   1757  CG1 VAL A 218       9.230  39.675  44.760  1.00 28.41           C  
ANISOU 1757  CG1 VAL A 218     3367   3379   4048   -327   -218   -434       C  
ATOM   1758  CG2 VAL A 218       8.769  40.996  42.671  1.00 31.97           C  
ANISOU 1758  CG2 VAL A 218     3833   3733   4580   -345   -133   -383       C  
ATOM   1759  N   ILE A 219      12.495  38.549  43.613  1.00 28.20           N  
ANISOU 1759  N   ILE A 219     3252   3377   4084   -333   -224   -424       N  
ATOM   1760  CA  ILE A 219      13.319  37.575  44.336  1.00 28.58           C  
ANISOU 1760  CA  ILE A 219     3277   3483   4101   -315   -266   -435       C  
ATOM   1761  C   ILE A 219      14.619  38.220  44.807  1.00 31.10           C  
ANISOU 1761  C   ILE A 219     3534   3815   4469   -338   -282   -493       C  
ATOM   1762  O   ILE A 219      15.030  38.061  45.965  1.00 29.70           O  
ANISOU 1762  O   ILE A 219     3330   3689   4265   -331   -327   -535       O  
ATOM   1763  CB  ILE A 219      13.572  36.340  43.449  1.00 30.35           C  
ANISOU 1763  CB  ILE A 219     3514   3711   4305   -291   -255   -378       C  
ATOM   1764  CG1 ILE A 219      12.282  35.542  43.283  1.00 25.53           C  
ANISOU 1764  CG1 ILE A 219     2960   3101   3638   -267   -251   -334       C  
ATOM   1765  CG2 ILE A 219      14.691  35.468  44.010  1.00 28.95           C  
ANISOU 1765  CG2 ILE A 219     3301   3584   4113   -273   -290   -388       C  
ATOM   1766  CD1 ILE A 219      12.357  34.542  42.103  1.00 26.91           C  
ANISOU 1766  CD1 ILE A 219     3154   3265   3807   -251   -226   -281       C  
ATOM   1767  N   PHE A 220      15.272  38.986  43.928  1.00 27.97           N  
ANISOU 1767  N   PHE A 220     3110   3373   4144   -366   -245   -496       N  
ATOM   1768  CA  PHE A 220      16.564  39.551  44.285  1.00 33.08           C  
ANISOU 1768  CA  PHE A 220     3692   4030   4847   -391   -257   -552       C  
ATOM   1769  C   PHE A 220      16.431  40.792  45.149  1.00 35.20           C  
ANISOU 1769  C   PHE A 220     3939   4288   5145   -422   -265   -623       C  
ATOM   1770  O   PHE A 220      17.361  41.109  45.898  1.00 35.91           O  
ANISOU 1770  O   PHE A 220     3974   4409   5259   -439   -295   -685       O  
ATOM   1771  CB  PHE A 220      17.389  39.823  43.024  1.00 35.44           C  
ANISOU 1771  CB  PHE A 220     3967   4284   5215   -408   -210   -528       C  
ATOM   1772  CG  PHE A 220      18.045  38.569  42.473  1.00 41.13           C  
ANISOU 1772  CG  PHE A 220     4683   5032   5914   -380   -215   -483       C  
ATOM   1773  CD1 PHE A 220      19.228  38.088  43.030  1.00 46.56           C  
ANISOU 1773  CD1 PHE A 220     5317   5767   6605   -375   -250   -511       C  
ATOM   1774  CD2 PHE A 220      17.458  37.847  41.449  1.00 43.42           C  
ANISOU 1774  CD2 PHE A 220     5020   5302   6174   -358   -186   -416       C  
ATOM   1775  CE1 PHE A 220      19.820  36.915  42.551  1.00 51.89           C  
ANISOU 1775  CE1 PHE A 220     5989   6465   7261   -347   -252   -469       C  
ATOM   1776  CE2 PHE A 220      18.044  36.682  40.960  1.00 44.51           C  
ANISOU 1776  CE2 PHE A 220     5157   5463   6294   -332   -188   -378       C  
ATOM   1777  CZ  PHE A 220      19.220  36.214  41.510  1.00 43.83           C  
ANISOU 1777  CZ  PHE A 220     5019   5419   6215   -326   -219   -403       C  
ATOM   1778  N   PHE A 221      15.292  41.471  45.104  1.00 30.98           N  
ANISOU 1778  N   PHE A 221     3446   3717   4610   -429   -241   -618       N  
ATOM   1779  CA  PHE A 221      15.043  42.510  46.097  1.00 33.17           C  
ANISOU 1779  CA  PHE A 221     3710   3991   4903   -452   -254   -688       C  
ATOM   1780  C   PHE A 221      14.926  41.895  47.481  1.00 33.90           C  
ANISOU 1780  C   PHE A 221     3801   4159   4921   -430   -316   -722       C  
ATOM   1781  O   PHE A 221      15.529  42.386  48.447  1.00 33.62           O  
ANISOU 1781  O   PHE A 221     3722   4155   4896   -447   -348   -796       O  
ATOM   1782  CB  PHE A 221      13.777  43.293  45.762  1.00 34.85           C  
ANISOU 1782  CB  PHE A 221     3969   4148   5125   -458   -213   -668       C  
ATOM   1783  CG  PHE A 221      13.308  44.181  46.891  1.00 40.88           C  
ANISOU 1783  CG  PHE A 221     4730   4914   5888   -474   -228   -736       C  
ATOM   1784  CD1 PHE A 221      12.382  43.724  47.815  1.00 45.50           C  
ANISOU 1784  CD1 PHE A 221     5349   5541   6396   -448   -262   -739       C  
ATOM   1785  CD2 PHE A 221      13.811  45.456  47.036  1.00 48.84           C  
ANISOU 1785  CD2 PHE A 221     5700   5881   6976   -515   -206   -799       C  
ATOM   1786  CE1 PHE A 221      11.964  44.526  48.857  1.00 48.97           C  
ANISOU 1786  CE1 PHE A 221     5788   5986   6833   -462   -275   -803       C  
ATOM   1787  CE2 PHE A 221      13.395  46.267  48.076  1.00 50.62           C  
ANISOU 1787  CE2 PHE A 221     5923   6109   7203   -531   -218   -867       C  
ATOM   1788  CZ  PHE A 221      12.470  45.802  48.986  1.00 48.58           C  
ANISOU 1788  CZ  PHE A 221     5701   5896   6862   -503   -254   -869       C  
ATOM   1789  N   CYS A 222      14.152  40.804  47.585  1.00 32.43           N  
ANISOU 1789  N   CYS A 222     3661   4004   4658   -391   -332   -670       N  
ATOM   1790  CA  CYS A 222      13.969  40.125  48.862  1.00 31.68           C  
ANISOU 1790  CA  CYS A 222     3572   3980   4487   -362   -385   -690       C  
ATOM   1791  C   CYS A 222      15.292  39.590  49.391  1.00 37.36           C  
ANISOU 1791  C   CYS A 222     4236   4760   5198   -353   -428   -719       C  
ATOM   1792  O   CYS A 222      15.606  39.753  50.580  1.00 34.56           O  
ANISOU 1792  O   CYS A 222     3855   4461   4815   -350   -473   -778       O  
ATOM   1793  CB  CYS A 222      12.940  38.996  48.714  1.00 25.38           C  
ANISOU 1793  CB  CYS A 222     2831   3192   3618   -323   -383   -620       C  
ATOM   1794  SG  CYS A 222      11.256  39.566  48.546  1.00 36.37           S  
ANISOU 1794  SG  CYS A 222     4282   4537   5000   -326   -349   -600       S  
ATOM   1795  N   TYR A 223      16.092  38.978  48.509  1.00 38.18           N  
ANISOU 1795  N   TYR A 223     4322   4857   5328   -348   -415   -680       N  
ATOM   1796  CA  TYR A 223      17.419  38.495  48.882  1.00 43.51           C  
ANISOU 1796  CA  TYR A 223     4940   5587   6005   -339   -452   -704       C  
ATOM   1797  C   TYR A 223      18.306  39.637  49.349  1.00 40.96           C  
ANISOU 1797  C   TYR A 223     4552   5268   5742   -379   -466   -790       C  
ATOM   1798  O   TYR A 223      19.005  39.515  50.363  1.00 46.76           O  
ANISOU 1798  O   TYR A 223     5243   6072   6453   -370   -518   -842       O  
ATOM   1799  CB  TYR A 223      18.054  37.756  47.692  1.00 51.53           C  
ANISOU 1799  CB  TYR A 223     5949   6581   7048   -330   -425   -645       C  
ATOM   1800  CG  TYR A 223      19.581  37.805  47.574  1.00 62.69           C  
ANISOU 1800  CG  TYR A 223     7290   8015   8513   -342   -437   -675       C  
ATOM   1801  CD1 TYR A 223      20.383  36.860  48.213  1.00 73.29           C  
ANISOU 1801  CD1 TYR A 223     8600   9430   9815   -308   -483   -676       C  
ATOM   1802  CD2 TYR A 223      20.214  38.767  46.783  1.00 68.93           C  
ANISOU 1802  CD2 TYR A 223     8044   8752   9394   -386   -399   -698       C  
ATOM   1803  CE1 TYR A 223      21.775  36.889  48.098  1.00 66.98           C  
ANISOU 1803  CE1 TYR A 223     7731   8654   9064   -317   -496   -704       C  
ATOM   1804  CE2 TYR A 223      21.606  38.806  46.661  1.00 74.23           C  
ANISOU 1804  CE2 TYR A 223     8645   9442  10117   -398   -407   -726       C  
ATOM   1805  CZ  TYR A 223      22.379  37.865  47.322  1.00 81.56           C  
ANISOU 1805  CZ  TYR A 223     9539  10446  11003   -365   -458   -730       C  
ATOM   1806  OH  TYR A 223      23.754  37.902  47.205  1.00 79.14           O  
ANISOU 1806  OH  TYR A 223     9159  10161  10750   -376   -467   -759       O  
ATOM   1807  N   GLY A 224      18.283  40.757  48.629  1.00 38.73           N  
ANISOU 1807  N   GLY A 224     4262   4914   5540   -423   -419   -808       N  
ATOM   1808  CA  GLY A 224      19.112  41.889  49.007  1.00 40.07           C  
ANISOU 1808  CA  GLY A 224     4368   5077   5780   -467   -424   -893       C  
ATOM   1809  C   GLY A 224      18.783  42.399  50.393  1.00 42.37           C  
ANISOU 1809  C   GLY A 224     4652   5413   6035   -471   -467   -969       C  
ATOM   1810  O   GLY A 224      19.675  42.811  51.140  1.00 44.26           O  
ANISOU 1810  O   GLY A 224     4829   5694   6294   -490   -503  -1048       O  
ATOM   1811  N   GLN A 225      17.497  42.386  50.751  1.00 36.01           N  
ANISOU 1811  N   GLN A 225     3908   4601   5174   -454   -463   -949       N  
ATOM   1812  CA  GLN A 225      17.100  42.725  52.115  1.00 43.95           C  
ANISOU 1812  CA  GLN A 225     4914   5656   6130   -449   -505  -1015       C  
ATOM   1813  C   GLN A 225      17.672  41.725  53.116  1.00 52.99           C  
ANISOU 1813  C   GLN A 225     6035   6903   7194   -408   -572  -1027       C  
ATOM   1814  O   GLN A 225      18.258  42.119  54.130  1.00 49.27           O  
ANISOU 1814  O   GLN A 225     5518   6489   6713   -417   -617  -1109       O  
ATOM   1815  CB  GLN A 225      15.576  42.788  52.218  1.00 44.78           C  
ANISOU 1815  CB  GLN A 225     5091   5732   6190   -434   -483   -980       C  
ATOM   1816  CG  GLN A 225      14.962  43.927  51.442  1.00 44.48           C  
ANISOU 1816  CG  GLN A 225     5074   5602   6226   -471   -421   -979       C  
ATOM   1817  CD  GLN A 225      15.381  45.282  51.972  1.00 54.31           C  
ANISOU 1817  CD  GLN A 225     6275   6826   7536   -517   -418  -1077       C  
ATOM   1818  OE1 GLN A 225      16.353  45.869  51.504  1.00 62.66           O  
ANISOU 1818  OE1 GLN A 225     7280   7852   8676   -554   -400  -1110       O  
ATOM   1819  NE2 GLN A 225      14.649  45.783  52.957  1.00 51.94           N  
ANISOU 1819  NE2 GLN A 225     5994   6541   7202   -517   -432  -1127       N  
ATOM   1820  N   LEU A 226      17.538  40.422  52.828  1.00 44.59           N  
ANISOU 1820  N   LEU A 226     5002   5864   6074   -363   -579   -946       N  
ATOM   1821  CA  LEU A 226      18.084  39.398  53.718  1.00 52.13           C  
ANISOU 1821  CA  LEU A 226     5938   6915   6955   -316   -636   -944       C  
ATOM   1822  C   LEU A 226      19.569  39.617  53.961  1.00 53.44           C  
ANISOU 1822  C   LEU A 226     6020   7126   7160   -332   -672  -1006       C  
ATOM   1823  O   LEU A 226      20.027  39.628  55.108  1.00 58.39           O  
ANISOU 1823  O   LEU A 226     6610   7833   7742   -317   -728  -1065       O  
ATOM   1824  CB  LEU A 226      17.864  37.998  53.138  1.00 47.57           C  
ANISOU 1824  CB  LEU A 226     5400   6340   6335   -271   -625   -846       C  
ATOM   1825  CG  LEU A 226      16.468  37.377  53.247  1.00 59.84           C  
ANISOU 1825  CG  LEU A 226     7032   7883   7823   -239   -608   -785       C  
ATOM   1826  CD1 LEU A 226      16.567  35.856  53.231  1.00 57.40           C  
ANISOU 1826  CD1 LEU A 226     6742   7612   7456   -185   -619   -711       C  
ATOM   1827  CD2 LEU A 226      15.763  37.859  54.492  1.00 53.18           C  
ANISOU 1827  CD2 LEU A 226     6205   7076   6926   -233   -634   -834       C  
ATOM   1828  N   VAL A 227      20.335  39.798  52.891  1.00 48.88           N  
ANISOU 1828  N   VAL A 227     5409   6500   6664   -360   -639   -993       N  
ATOM   1829  CA  VAL A 227      21.782  39.907  53.017  1.00 50.25           C  
ANISOU 1829  CA  VAL A 227     5498   6714   6880   -374   -669  -1044       C  
ATOM   1830  C   VAL A 227      22.175  41.251  53.605  1.00 59.08           C  
ANISOU 1830  C   VAL A 227     6562   7832   8053   -426   -682  -1154       C  
ATOM   1831  O   VAL A 227      22.827  41.314  54.651  1.00 62.86           O  
ANISOU 1831  O   VAL A 227     6988   8393   8504   -419   -742  -1226       O  
ATOM   1832  CB  VAL A 227      22.467  39.689  51.659  1.00 58.30           C  
ANISOU 1832  CB  VAL A 227     6499   7678   7974   -389   -624   -994       C  
ATOM   1833  CG1 VAL A 227      23.908  40.178  51.734  1.00 49.07           C  
ANISOU 1833  CG1 VAL A 227     5236   6534   6874   -420   -644  -1063       C  
ATOM   1834  CG2 VAL A 227      22.414  38.223  51.271  1.00 59.39           C  
ANISOU 1834  CG2 VAL A 227     6672   7840   8055   -334   -625   -901       C  
ATOM   1835  N   PHE A 228      21.815  42.337  52.926  1.00 52.51           N  
ANISOU 1835  N   PHE A 228     5741   6909   7303   -476   -626  -1172       N  
ATOM   1836  CA  PHE A 228      22.315  43.663  53.289  1.00 66.96           C  
ANISOU 1836  CA  PHE A 228     7513   8720   9208   -534   -626  -1277       C  
ATOM   1837  C   PHE A 228      21.456  44.321  54.363  1.00 63.43           C  
ANISOU 1837  C   PHE A 228     7091   8290   8718   -539   -646  -1340       C  
ATOM   1838  O   PHE A 228      21.100  45.493  54.260  1.00 84.63           O  
ANISOU 1838  O   PHE A 228     9779  10910  11468   -585   -608  -1388       O  
ATOM   1839  CB  PHE A 228      22.401  44.537  52.041  1.00 55.97           C  
ANISOU 1839  CB  PHE A 228     6117   7218   7930   -584   -549  -1263       C  
ATOM   1840  N   THR A 229      21.144  43.570  55.419  1.00 75.05           N  
ANISOU 1840  N   THR A 229     8582   9852  10081   -490   -704  -1340       N  
ATOM   1841  CA  THR A 229      20.483  44.096  56.618  1.00 83.93           C  
ANISOU 1841  CA  THR A 229     9723  11014  11152   -488   -734  -1408       C  
ATOM   1842  C   THR A 229      20.931  43.280  57.826  1.00 79.68           C  
ANISOU 1842  C   THR A 229     9160  10603  10512   -438   -813  -1433       C  
ATOM   1843  O   THR A 229      20.665  42.079  57.904  1.00 75.54           O  
ANISOU 1843  O   THR A 229     8673  10121   9908   -379   -829  -1352       O  
ATOM   1844  CB  THR A 229      18.920  44.055  56.553  1.00 82.00           C  
ANISOU 1844  CB  THR A 229     9570  10724  10861   -469   -698  -1350       C  
ATOM   1845  OG1 THR A 229      18.463  42.704  56.408  1.00 83.01           O  
ANISOU 1845  OG1 THR A 229     9748  10883  10909   -410   -706  -1250       O  
ATOM   1846  CG2 THR A 229      18.359  44.925  55.424  1.00 72.56           C  
ANISOU 1846  CG2 THR A 229     8403   9408   9758   -512   -620  -1325       C  
ATOM   1847  N   LYS A 245      17.960  28.098  64.001  1.00 62.09           N  
ANISOU 1847  N   LYS A 245     7358   9045   7191    448   -964   -518       N  
ATOM   1848  CA  LYS A 245      18.478  26.986  63.206  1.00 66.75           C  
ANISOU 1848  CA  LYS A 245     7946   9603   7814    474   -937   -438       C  
ATOM   1849  C   LYS A 245      17.417  26.490  62.250  1.00 57.95           C  
ANISOU 1849  C   LYS A 245     6898   8376   6744    451   -864   -369       C  
ATOM   1850  O   LYS A 245      17.705  26.152  61.095  1.00 55.30           O  
ANISOU 1850  O   LYS A 245     6557   7973   6479    426   -832   -338       O  
ATOM   1851  CB  LYS A 245      18.946  25.833  64.099  1.00 61.66           C  
ANISOU 1851  CB  LYS A 245     7298   9047   7083    571   -958   -375       C  
ATOM   1852  CG  LYS A 245      20.374  25.974  64.595  1.00 66.68           C  
ANISOU 1852  CG  LYS A 245     7851   9786   7699    599  -1028   -421       C  
ATOM   1853  CD  LYS A 245      20.854  24.691  65.258  1.00 73.19           C  
ANISOU 1853  CD  LYS A 245     8674  10685   8449    700  -1039   -340       C  
ATOM   1854  N   ALA A 246      16.183  26.432  62.756  1.00 57.61           N  
ANISOU 1854  N   ALA A 246     6915   8318   6654    462   -837   -348       N  
ATOM   1855  CA  ALA A 246      15.065  25.974  61.943  1.00 59.54           C  
ANISOU 1855  CA  ALA A 246     7224   8463   6937    440   -769   -288       C  
ATOM   1856  C   ALA A 246      14.817  26.921  60.778  1.00 44.66           C  
ANISOU 1856  C   ALA A 246     5333   6492   5143    355   -748   -332       C  
ATOM   1857  O   ALA A 246      14.659  26.488  59.630  1.00 46.56           O  
ANISOU 1857  O   ALA A 246     5591   6656   5444    331   -706   -291       O  
ATOM   1858  CB  ALA A 246      13.813  25.838  62.810  1.00 69.60           C  
ANISOU 1858  CB  ALA A 246     8557   9745   8144    467   -747   -265       C  
ATOM   1859  N   GLU A 247      14.786  28.226  61.049  1.00 44.73           N  
ANISOU 1859  N   GLU A 247     5319   6514   5164    310   -776   -418       N  
ATOM   1860  CA  GLU A 247      14.564  29.158  59.953  1.00 53.03           C  
ANISOU 1860  CA  GLU A 247     6364   7482   6302    234   -752   -456       C  
ATOM   1861  C   GLU A 247      15.752  29.182  59.008  1.00 41.72           C  
ANISOU 1861  C   GLU A 247     4880   6033   4940    210   -760   -465       C  
ATOM   1862  O   GLU A 247      15.568  29.304  57.796  1.00 36.30           O  
ANISOU 1862  O   GLU A 247     4204   5266   4324    167   -721   -448       O  
ATOM   1863  CB  GLU A 247      14.269  30.559  60.487  1.00 52.53           C  
ANISOU 1863  CB  GLU A 247     6289   7430   6240    193   -775   -545       C  
ATOM   1864  CG  GLU A 247      12.974  30.661  61.288  1.00 54.88           C  
ANISOU 1864  CG  GLU A 247     6642   7733   6479    209   -760   -539       C  
ATOM   1865  CD  GLU A 247      11.703  30.519  60.451  1.00 53.59           C  
ANISOU 1865  CD  GLU A 247     6536   7476   6351    183   -698   -490       C  
ATOM   1866  OE1 GLU A 247      11.758  30.131  59.255  1.00 49.65           O  
ANISOU 1866  OE1 GLU A 247     6042   6912   5913    161   -666   -449       O  
ATOM   1867  OE2 GLU A 247      10.626  30.798  61.011  1.00 62.03           O  
ANISOU 1867  OE2 GLU A 247     7645   8539   7386    185   -683   -494       O  
ATOM   1868  N   LYS A 248      16.966  29.032  59.547  1.00 36.11           N  
ANISOU 1868  N   LYS A 248     4112   5400   4207    240   -808   -488       N  
ATOM   1869  CA  LYS A 248      18.162  29.024  58.712  1.00 40.02           C  
ANISOU 1869  CA  LYS A 248     4552   5884   4769    221   -815   -497       C  
ATOM   1870  C   LYS A 248      18.128  27.875  57.709  1.00 34.60           C  
ANISOU 1870  C   LYS A 248     3894   5142   4111    238   -768   -410       C  
ATOM   1871  O   LYS A 248      18.542  28.041  56.553  1.00 33.29           O  
ANISOU 1871  O   LYS A 248     3710   4918   4020    199   -744   -409       O  
ATOM   1872  CB  LYS A 248      19.408  28.933  59.596  1.00 40.59           C  
ANISOU 1872  CB  LYS A 248     4558   6062   4803    260   -878   -532       C  
ATOM   1873  CG  LYS A 248      20.721  28.998  58.845  1.00 46.45           C  
ANISOU 1873  CG  LYS A 248     5233   6803   5615    241   -890   -550       C  
ATOM   1874  CD  LYS A 248      21.924  28.920  59.805  1.00 47.64           C  
ANISOU 1874  CD  LYS A 248     5311   7067   5722    283   -958   -589       C  
ATOM   1875  CE  LYS A 248      22.054  27.538  60.429  1.00 61.78           C  
ANISOU 1875  CE  LYS A 248     7121   8919   7435    373   -966   -508       C  
ATOM   1876  NZ  LYS A 248      23.254  27.428  61.310  1.00 67.13           N  
ANISOU 1876  NZ  LYS A 248     7724   9713   8068    420  -1034   -542       N  
ATOM   1877  N   GLU A 249      17.652  26.697  58.136  1.00 34.34           N  
ANISOU 1877  N   GLU A 249     3905   5124   4020    298   -751   -336       N  
ATOM   1878  CA  GLU A 249      17.552  25.562  57.223  1.00 37.49           C  
ANISOU 1878  CA  GLU A 249     4334   5464   4445    314   -703   -257       C  
ATOM   1879  C   GLU A 249      16.644  25.888  56.042  1.00 33.25           C  
ANISOU 1879  C   GLU A 249     3837   4827   3969    255   -651   -250       C  
ATOM   1880  O   GLU A 249      16.955  25.549  54.890  1.00 30.19           O  
ANISOU 1880  O   GLU A 249     3446   4385   3638    236   -620   -224       O  
ATOM   1881  CB  GLU A 249      17.038  24.323  57.966  1.00 39.43           C  
ANISOU 1881  CB  GLU A 249     4625   5736   4621    385   -686   -183       C  
ATOM   1882  CG  GLU A 249      17.065  23.026  57.137  1.00 42.48           C  
ANISOU 1882  CG  GLU A 249     5037   6069   5034    409   -636   -102       C  
ATOM   1883  CD  GLU A 249      16.303  21.859  57.791  1.00 42.02           C  
ANISOU 1883  CD  GLU A 249     5034   6014   4918    470   -605    -27       C  
ATOM   1884  OE1 GLU A 249      15.169  22.079  58.264  1.00 50.14           O  
ANISOU 1884  OE1 GLU A 249     6105   7031   5914    463   -590    -28       O  
ATOM   1885  OE2 GLU A 249      16.841  20.731  57.833  1.00 37.99           O  
ANISOU 1885  OE2 GLU A 249     4521   5516   4396    524   -591     33       O  
ATOM   1886  N   VAL A 250      15.513  26.542  56.313  1.00 28.88           N  
ANISOU 1886  N   VAL A 250     3320   4251   3401    229   -641   -272       N  
ATOM   1887  CA  VAL A 250      14.588  26.917  55.252  1.00 32.58           C  
ANISOU 1887  CA  VAL A 250     3826   4633   3922    177   -596   -267       C  
ATOM   1888  C   VAL A 250      15.217  27.952  54.327  1.00 29.44           C  
ANISOU 1888  C   VAL A 250     3387   4201   3598    119   -598   -317       C  
ATOM   1889  O   VAL A 250      15.096  27.870  53.101  1.00 25.85           O  
ANISOU 1889  O   VAL A 250     2944   3680   3198     90   -561   -295       O  
ATOM   1890  CB  VAL A 250      13.270  27.438  55.857  1.00 30.97           C  
ANISOU 1890  CB  VAL A 250     3664   4420   3683    167   -587   -282       C  
ATOM   1891  CG1 VAL A 250      12.357  27.942  54.758  1.00 32.46           C  
ANISOU 1891  CG1 VAL A 250     3882   4524   3926    114   -546   -281       C  
ATOM   1892  CG2 VAL A 250      12.582  26.329  56.674  1.00 33.60           C  
ANISOU 1892  CG2 VAL A 250     4041   4776   3948    224   -573   -223       C  
ATOM   1893  N   THR A 251      15.852  28.974  54.900  1.00 25.61           N  
ANISOU 1893  N   THR A 251     2854   3758   3118    101   -640   -388       N  
ATOM   1894  CA  THR A 251      16.461  30.013  54.071  1.00 28.74           C  
ANISOU 1894  CA  THR A 251     3210   4119   3592     44   -637   -437       C  
ATOM   1895  C   THR A 251      17.546  29.427  53.169  1.00 30.60           C  
ANISOU 1895  C   THR A 251     3412   4342   3873     49   -627   -409       C  
ATOM   1896  O   THR A 251      17.646  29.780  51.990  1.00 27.64           O  
ANISOU 1896  O   THR A 251     3033   3904   3562      9   -594   -406       O  
ATOM   1897  CB  THR A 251      17.037  31.117  54.967  1.00 36.06           C  
ANISOU 1897  CB  THR A 251     4087   5100   4516     27   -685   -523       C  
ATOM   1898  OG1 THR A 251      16.014  31.589  55.858  1.00 32.01           O  
ANISOU 1898  OG1 THR A 251     3608   4600   3954     28   -692   -548       O  
ATOM   1899  CG2 THR A 251      17.548  32.276  54.127  1.00 32.99           C  
ANISOU 1899  CG2 THR A 251     3658   4662   4214    -36   -673   -575       C  
ATOM   1900  N   ARG A 252      18.350  28.513  53.710  1.00 23.72           N  
ANISOU 1900  N   ARG A 252     2516   3531   2965    100   -653   -385       N  
ATOM   1901  CA  ARG A 252      19.370  27.852  52.911  1.00 29.16           C  
ANISOU 1901  CA  ARG A 252     3174   4211   3694    111   -642   -354       C  
ATOM   1902  C   ARG A 252      18.745  27.068  51.772  1.00 30.97           C  
ANISOU 1902  C   ARG A 252     3454   4366   3946    108   -585   -288       C  
ATOM   1903  O   ARG A 252      19.234  27.114  50.641  1.00 29.21           O  
ANISOU 1903  O   ARG A 252     3217   4099   3782     83   -558   -281       O  
ATOM   1904  CB  ARG A 252      20.206  26.936  53.795  1.00 26.91           C  
ANISOU 1904  CB  ARG A 252     2860   4008   3358    176   -679   -332       C  
ATOM   1905  CG  ARG A 252      21.122  27.712  54.683  1.00 25.93           C  
ANISOU 1905  CG  ARG A 252     2667   3961   3225    175   -739   -404       C  
ATOM   1906  CD  ARG A 252      21.781  26.806  55.681  1.00 30.59           C  
ANISOU 1906  CD  ARG A 252     3233   4641   3749    248   -778   -379       C  
ATOM   1907  NE  ARG A 252      22.869  27.501  56.350  1.00 37.00           N  
ANISOU 1907  NE  ARG A 252     3967   5531   4562    245   -838   -451       N  
ATOM   1908  CZ  ARG A 252      23.669  26.928  57.238  1.00 43.48           C  
ANISOU 1908  CZ  ARG A 252     4746   6444   5329    306   -884   -446       C  
ATOM   1909  NH1 ARG A 252      23.507  25.663  57.599  1.00 40.11           N  
ANISOU 1909  NH1 ARG A 252     4354   6042   4844    377   -875   -366       N  
ATOM   1910  NH2 ARG A 252      24.658  27.637  57.768  1.00 49.37           N  
ANISOU 1910  NH2 ARG A 252     5414   7261   6082    296   -940   -521       N  
ATOM   1911  N   MET A 253      17.660  26.345  52.040  1.00 25.53           N  
ANISOU 1911  N   MET A 253     2825   3663   3210    134   -564   -243       N  
ATOM   1912  CA  MET A 253      17.049  25.588  50.956  1.00 23.23           C  
ANISOU 1912  CA  MET A 253     2580   3303   2942    129   -510   -188       C  
ATOM   1913  C   MET A 253      16.521  26.507  49.860  1.00 28.16           C  
ANISOU 1913  C   MET A 253     3218   3862   3621     69   -481   -211       C  
ATOM   1914  O   MET A 253      16.642  26.204  48.664  1.00 23.42           O  
ANISOU 1914  O   MET A 253     2625   3212   3062     53   -446   -186       O  
ATOM   1915  CB  MET A 253      15.922  24.701  51.485  1.00 21.98           C  
ANISOU 1915  CB  MET A 253     2481   3140   2730    163   -491   -141       C  
ATOM   1916  CG  MET A 253      15.190  23.978  50.328  1.00 24.90           C  
ANISOU 1916  CG  MET A 253     2897   3437   3128    150   -436    -96       C  
ATOM   1917  SD  MET A 253      14.130  22.694  51.017  1.00 29.68           S  
ANISOU 1917  SD  MET A 253     3560   4039   3678    197   -410    -36       S  
ATOM   1918  CE  MET A 253      12.973  22.520  49.643  1.00 27.14           C  
ANISOU 1918  CE  MET A 253     3285   3630   3397    154   -355    -19       C  
ATOM   1919  N   VAL A 254      15.891  27.618  50.237  1.00 23.90           N  
ANISOU 1919  N   VAL A 254     2683   3318   3079     37   -493   -256       N  
ATOM   1920  CA  VAL A 254      15.338  28.484  49.196  1.00 27.01           C  
ANISOU 1920  CA  VAL A 254     3092   3649   3523    -14   -462   -270       C  
ATOM   1921  C   VAL A 254      16.451  29.062  48.330  1.00 28.82           C  
ANISOU 1921  C   VAL A 254     3273   3861   3818    -44   -456   -293       C  
ATOM   1922  O   VAL A 254      16.271  29.264  47.118  1.00 26.15           O  
ANISOU 1922  O   VAL A 254     2948   3466   3522    -71   -419   -278       O  
ATOM   1923  CB  VAL A 254      14.466  29.578  49.848  1.00 32.84           C  
ANISOU 1923  CB  VAL A 254     3843   4387   4247    -39   -473   -313       C  
ATOM   1924  CG1 VAL A 254      14.023  30.629  48.809  1.00 28.73           C  
ANISOU 1924  CG1 VAL A 254     3330   3804   3783    -89   -442   -330       C  
ATOM   1925  CG2 VAL A 254      13.270  28.916  50.506  1.00 27.26           C  
ANISOU 1925  CG2 VAL A 254     3188   3687   3481    -10   -467   -281       C  
ATOM   1926  N   ILE A 255      17.616  29.326  48.919  1.00 25.36           N  
ANISOU 1926  N   ILE A 255     2778   3472   3388    -38   -493   -329       N  
ATOM   1927  CA  ILE A 255      18.740  29.828  48.126  1.00 30.45           C  
ANISOU 1927  CA  ILE A 255     3371   4100   4099    -65   -485   -350       C  
ATOM   1928  C   ILE A 255      19.103  28.829  47.027  1.00 25.55           C  
ANISOU 1928  C   ILE A 255     2761   3449   3498    -49   -449   -294       C  
ATOM   1929  O   ILE A 255      19.320  29.202  45.869  1.00 23.40           O  
ANISOU 1929  O   ILE A 255     2484   3127   3279    -79   -414   -290       O  
ATOM   1930  CB  ILE A 255      19.954  30.124  49.027  1.00 26.87           C  
ANISOU 1930  CB  ILE A 255     2849   3714   3648    -56   -534   -399       C  
ATOM   1931  CG1 ILE A 255      19.715  31.367  49.877  1.00 33.65           C  
ANISOU 1931  CG1 ILE A 255     3688   4592   4505    -86   -563   -470       C  
ATOM   1932  CG2 ILE A 255      21.219  30.298  48.177  1.00 35.50           C  
ANISOU 1932  CG2 ILE A 255     3886   4793   4809    -74   -522   -408       C  
ATOM   1933  CD1 ILE A 255      20.779  31.546  50.979  1.00 36.01           C  
ANISOU 1933  CD1 ILE A 255     3922   4973   4789    -70   -621   -523       C  
ATOM   1934  N   ILE A 256      19.163  27.543  47.378  1.00 24.77           N  
ANISOU 1934  N   ILE A 256     2677   3377   3356      0   -454   -250       N  
ATOM   1935  CA  ILE A 256      19.528  26.512  46.410  1.00 23.40           C  
ANISOU 1935  CA  ILE A 256     2515   3176   3201     18   -420   -200       C  
ATOM   1936  C   ILE A 256      18.427  26.344  45.374  1.00 21.03           C  
ANISOU 1936  C   ILE A 256     2273   2811   2907     -2   -373   -170       C  
ATOM   1937  O   ILE A 256      18.707  26.120  44.189  1.00 22.57           O  
ANISOU 1937  O   ILE A 256     2471   2966   3138    -13   -337   -150       O  
ATOM   1938  CB  ILE A 256      19.838  25.189  47.132  1.00 27.50           C  
ANISOU 1938  CB  ILE A 256     3037   3739   3674     78   -434   -160       C  
ATOM   1939  CG1 ILE A 256      21.062  25.366  48.031  1.00 23.73           C  
ANISOU 1939  CG1 ILE A 256     2493   3333   3192    100   -482   -190       C  
ATOM   1940  CG2 ILE A 256      20.068  24.062  46.137  1.00 25.71           C  
ANISOU 1940  CG2 ILE A 256     2828   3474   3465     97   -391   -108       C  
ATOM   1941  CD1 ILE A 256      22.325  25.849  47.278  1.00 28.44           C  
ANISOU 1941  CD1 ILE A 256     3029   3923   3856     76   -479   -214       C  
ATOM   1942  N   MET A 257      17.156  26.457  45.792  1.00 21.44           N  
ANISOU 1942  N   MET A 257     2371   2854   2923     -6   -372   -168       N  
ATOM   1943  CA  MET A 257      16.063  26.371  44.819  1.00 20.75           C  
ANISOU 1943  CA  MET A 257     2333   2709   2840    -26   -332   -146       C  
ATOM   1944  C   MET A 257      16.174  27.474  43.777  1.00 24.34           C  
ANISOU 1944  C   MET A 257     2776   3126   3348    -70   -311   -168       C  
ATOM   1945  O   MET A 257      15.909  27.246  42.593  1.00 21.53           O  
ANISOU 1945  O   MET A 257     2443   2729   3010    -80   -274   -144       O  
ATOM   1946  CB  MET A 257      14.697  26.456  45.519  1.00 23.18           C  
ANISOU 1946  CB  MET A 257     2684   3018   3106    -25   -337   -145       C  
ATOM   1947  CG  MET A 257      14.341  25.245  46.344  1.00 26.29           C  
ANISOU 1947  CG  MET A 257     3104   3436   3450     19   -341   -111       C  
ATOM   1948  SD  MET A 257      12.828  25.535  47.296  1.00 27.88           S  
ANISOU 1948  SD  MET A 257     3346   3642   3604     18   -348   -117       S  
ATOM   1949  CE  MET A 257      11.631  25.366  45.994  1.00 22.70           C  
ANISOU 1949  CE  MET A 257     2736   2921   2968    -10   -302    -96       C  
ATOM   1950  N   VAL A 258      16.571  28.677  44.190  1.00 21.85           N  
ANISOU 1950  N   VAL A 258     2425   2822   3056    -95   -332   -213       N  
ATOM   1951  CA  VAL A 258      16.710  29.747  43.200  1.00 22.18           C  
ANISOU 1951  CA  VAL A 258     2454   2822   3152   -135   -305   -230       C  
ATOM   1952  C   VAL A 258      17.899  29.496  42.279  1.00 22.26           C  
ANISOU 1952  C   VAL A 258     2431   2820   3206   -136   -284   -217       C  
ATOM   1953  O   VAL A 258      17.799  29.683  41.057  1.00 23.90           O  
ANISOU 1953  O   VAL A 258     2652   2985   3442   -152   -244   -199       O  
ATOM   1954  CB  VAL A 258      16.814  31.110  43.899  1.00 23.37           C  
ANISOU 1954  CB  VAL A 258     2574   2980   3324   -164   -327   -285       C  
ATOM   1955  CG1 VAL A 258      17.162  32.195  42.876  1.00 27.62           C  
ANISOU 1955  CG1 VAL A 258     3093   3472   3928   -203   -293   -298       C  
ATOM   1956  CG2 VAL A 258      15.474  31.411  44.598  1.00 26.88           C  
ANISOU 1956  CG2 VAL A 258     3060   3426   3728   -166   -337   -293       C  
ATOM   1957  N   ILE A 259      19.042  29.085  42.841  1.00 20.95           N  
ANISOU 1957  N   ILE A 259     2219   2696   3045   -116   -310   -227       N  
ATOM   1958  CA  ILE A 259      20.188  28.761  41.994  1.00 22.17           C  
ANISOU 1958  CA  ILE A 259     2340   2842   3242   -113   -288   -213       C  
ATOM   1959  C   ILE A 259      19.827  27.647  41.012  1.00 24.31           C  
ANISOU 1959  C   ILE A 259     2655   3084   3498    -93   -250   -161       C  
ATOM   1960  O   ILE A 259      20.124  27.738  39.811  1.00 22.09           O  
ANISOU 1960  O   ILE A 259     2374   2766   3251   -106   -211   -146       O  
ATOM   1961  CB  ILE A 259      21.406  28.380  42.856  1.00 21.59           C  
ANISOU 1961  CB  ILE A 259     2209   2824   3169    -88   -326   -229       C  
ATOM   1962  CG1 ILE A 259      21.913  29.605  43.615  1.00 23.21           C  
ANISOU 1962  CG1 ILE A 259     2361   3055   3402   -116   -359   -291       C  
ATOM   1963  CG2 ILE A 259      22.532  27.806  41.970  1.00 25.24           C  
ANISOU 1963  CG2 ILE A 259     2641   3278   3671    -77   -300   -205       C  
ATOM   1964  CD1 ILE A 259      23.029  29.307  44.582  1.00 26.89           C  
ANISOU 1964  CD1 ILE A 259     2767   3588   3862    -91   -405   -315       C  
ATOM   1965  N   ALA A 260      19.157  26.592  41.499  1.00 20.46           N  
ANISOU 1965  N   ALA A 260     2206   2610   2959    -61   -259   -134       N  
ATOM   1966  CA  ALA A 260      18.808  25.465  40.627  1.00 20.54           C  
ANISOU 1966  CA  ALA A 260     2256   2592   2958    -43   -222    -91       C  
ATOM   1967  C   ALA A 260      17.886  25.917  39.508  1.00 23.41           C  
ANISOU 1967  C   ALA A 260     2659   2908   3328    -72   -188    -85       C  
ATOM   1968  O   ALA A 260      17.976  25.429  38.365  1.00 20.95           O  
ANISOU 1968  O   ALA A 260     2363   2569   3029    -70   -151    -63       O  
ATOM   1969  CB  ALA A 260      18.146  24.347  41.444  1.00 21.65           C  
ANISOU 1969  CB  ALA A 260     2431   2750   3047     -8   -234    -66       C  
ATOM   1970  N   PHE A 261      16.947  26.808  39.831  1.00 19.66           N  
ANISOU 1970  N   PHE A 261     2201   2427   2842    -94   -198   -105       N  
ATOM   1971  CA  PHE A 261      16.030  27.320  38.810  1.00 19.92           C  
ANISOU 1971  CA  PHE A 261     2268   2421   2880   -118   -168    -98       C  
ATOM   1972  C   PHE A 261      16.788  28.054  37.708  1.00 19.53           C  
ANISOU 1972  C   PHE A 261     2195   2347   2879   -138   -138   -100       C  
ATOM   1973  O   PHE A 261      16.516  27.869  36.512  1.00 19.96           O  
ANISOU 1973  O   PHE A 261     2274   2374   2935   -140   -102    -78       O  
ATOM   1974  CB  PHE A 261      14.996  28.261  39.444  1.00 23.82           C  
ANISOU 1974  CB  PHE A 261     2778   2914   3360   -137   -185   -120       C  
ATOM   1975  CG  PHE A 261      13.993  28.771  38.447  1.00 22.28           C  
ANISOU 1975  CG  PHE A 261     2616   2683   3164   -155   -156   -110       C  
ATOM   1976  CD1 PHE A 261      14.250  29.907  37.689  1.00 24.32           C  
ANISOU 1976  CD1 PHE A 261     2861   2917   3463   -179   -134   -117       C  
ATOM   1977  CD2 PHE A 261      12.816  28.077  38.234  1.00 23.03           C  
ANISOU 1977  CD2 PHE A 261     2756   2771   3222   -146   -148    -91       C  
ATOM   1978  CE1 PHE A 261      13.342  30.342  36.726  1.00 24.77           C  
ANISOU 1978  CE1 PHE A 261     2950   2947   3516   -188   -106   -102       C  
ATOM   1979  CE2 PHE A 261      11.898  28.522  37.275  1.00 25.30           C  
ANISOU 1979  CE2 PHE A 261     3071   3034   3507   -160   -124    -82       C  
ATOM   1980  CZ  PHE A 261      12.175  29.630  36.520  1.00 20.75           C  
ANISOU 1980  CZ  PHE A 261     2482   2438   2964   -177   -105    -85       C  
ATOM   1981  N   LEU A 262      17.739  28.901  38.084  1.00 19.70           N  
ANISOU 1981  N   LEU A 262     2167   2377   2939   -153   -150   -127       N  
ATOM   1982  CA  LEU A 262      18.488  29.632  37.062  1.00 21.33           C  
ANISOU 1982  CA  LEU A 262     2348   2556   3198   -172   -115   -127       C  
ATOM   1983  C   LEU A 262      19.330  28.694  36.209  1.00 25.71           C  
ANISOU 1983  C   LEU A 262     2896   3108   3764   -153    -88   -100       C  
ATOM   1984  O   LEU A 262      19.437  28.874  34.991  1.00 23.15           O  
ANISOU 1984  O   LEU A 262     2583   2756   3459   -160    -47    -81       O  
ATOM   1985  CB  LEU A 262      19.355  30.696  37.727  1.00 21.87           C  
ANISOU 1985  CB  LEU A 262     2361   2636   3314   -195   -133   -168       C  
ATOM   1986  CG  LEU A 262      18.512  31.767  38.406  1.00 27.00           C  
ANISOU 1986  CG  LEU A 262     3020   3279   3960   -218   -150   -198       C  
ATOM   1987  CD1 LEU A 262      19.457  32.674  39.204  1.00 29.62           C  
ANISOU 1987  CD1 LEU A 262     3291   3626   4337   -240   -172   -247       C  
ATOM   1988  CD2 LEU A 262      17.678  32.541  37.382  1.00 28.69           C  
ANISOU 1988  CD2 LEU A 262     3268   3446   4185   -235   -108   -180       C  
ATOM   1989  N   ILE A 263      19.945  27.681  36.822  1.00 20.39           N  
ANISOU 1989  N   ILE A 263     2206   2465   3077   -126   -110    -95       N  
ATOM   1990  CA  ILE A 263      20.711  26.733  36.018  1.00 20.22           C  
ANISOU 1990  CA  ILE A 263     2180   2438   3066   -104    -81    -69       C  
ATOM   1991  C   ILE A 263      19.794  26.067  35.008  1.00 22.72           C  
ANISOU 1991  C   ILE A 263     2554   2728   3352    -98    -49    -41       C  
ATOM   1992  O   ILE A 263      20.139  25.900  33.835  1.00 21.31           O  
ANISOU 1992  O   ILE A 263     2381   2528   3189    -97     -9    -24       O  
ATOM   1993  CB  ILE A 263      21.390  25.687  36.922  1.00 20.62           C  
ANISOU 1993  CB  ILE A 263     2206   2525   3102    -70   -110    -64       C  
ATOM   1994  CG1 ILE A 263      22.547  26.305  37.702  1.00 27.53           C  
ANISOU 1994  CG1 ILE A 263     3014   3434   4013    -75   -140    -93       C  
ATOM   1995  CG2 ILE A 263      21.876  24.544  36.098  1.00 21.37           C  
ANISOU 1995  CG2 ILE A 263     2311   2608   3199    -44    -76    -32       C  
ATOM   1996  CD1 ILE A 263      23.153  25.340  38.699  1.00 31.49           C  
ANISOU 1996  CD1 ILE A 263     3490   3980   4493    -35   -173    -87       C  
ATOM   1997  N   CYS A 264      18.601  25.693  35.458  1.00 19.53           N  
ANISOU 1997  N   CYS A 264     2191   2326   2904    -93    -64    -38       N  
ATOM   1998  CA  CYS A 264      17.678  24.941  34.631  1.00 22.37           C  
ANISOU 1998  CA  CYS A 264     2602   2665   3232    -86    -39    -19       C  
ATOM   1999  C   CYS A 264      17.163  25.772  33.458  1.00 24.90           C  
ANISOU 1999  C   CYS A 264     2942   2961   3559   -108     -9    -16       C  
ATOM   2000  O   CYS A 264      17.122  25.289  32.323  1.00 24.53           O  
ANISOU 2000  O   CYS A 264     2917   2900   3506   -102     24     -1       O  
ATOM   2001  CB  CYS A 264      16.533  24.449  35.525  1.00 22.79           C  
ANISOU 2001  CB  CYS A 264     2687   2728   3243    -79    -64    -20       C  
ATOM   2002  SG  CYS A 264      15.331  23.418  34.651  1.00 24.32           S  
ANISOU 2002  SG  CYS A 264     2938   2899   3402    -74    -36     -4       S  
ATOM   2003  N   TRP A 265      16.790  27.029  33.697  1.00 19.05           N  
ANISOU 2003  N   TRP A 265     2194   2215   2829   -131    -19    -31       N  
ATOM   2004  CA  TRP A 265      16.000  27.776  32.725  1.00 20.69           C  
ANISOU 2004  CA  TRP A 265     2428   2402   3031   -145      6    -23       C  
ATOM   2005  C   TRP A 265      16.757  28.883  31.996  1.00 19.46           C  
ANISOU 2005  C   TRP A 265     2246   2227   2920   -160     36    -20       C  
ATOM   2006  O   TRP A 265      16.288  29.334  30.948  1.00 24.60           O  
ANISOU 2006  O   TRP A 265     2920   2862   3566   -162     67     -4       O  
ATOM   2007  CB  TRP A 265      14.777  28.394  33.428  1.00 18.73           C  
ANISOU 2007  CB  TRP A 265     2200   2156   2762   -157    -19    -36       C  
ATOM   2008  CG  TRP A 265      13.752  27.364  33.748  1.00 18.35           C  
ANISOU 2008  CG  TRP A 265     2188   2118   2667   -144    -33    -32       C  
ATOM   2009  CD1 TRP A 265      13.492  26.801  34.966  1.00 21.16           C  
ANISOU 2009  CD1 TRP A 265     2545   2492   3004   -136    -65    -40       C  
ATOM   2010  CD2 TRP A 265      12.862  26.747  32.821  1.00 20.12           C  
ANISOU 2010  CD2 TRP A 265     2450   2335   2860   -139    -15    -19       C  
ATOM   2011  NE1 TRP A 265      12.498  25.853  34.841  1.00 19.56           N  
ANISOU 2011  NE1 TRP A 265     2379   2287   2766   -126    -62    -31       N  
ATOM   2012  CE2 TRP A 265      12.091  25.812  33.535  1.00 19.34           C  
ANISOU 2012  CE2 TRP A 265     2372   2244   2730   -130    -33    -22       C  
ATOM   2013  CE3 TRP A 265      12.670  26.871  31.441  1.00 18.15           C  
ANISOU 2013  CE3 TRP A 265     2217   2074   2604   -138     17     -6       C  
ATOM   2014  CZ2 TRP A 265      11.124  25.019  32.919  1.00 19.16           C  
ANISOU 2014  CZ2 TRP A 265     2384   2217   2678   -126    -22    -18       C  
ATOM   2015  CZ3 TRP A 265      11.680  26.094  30.837  1.00 17.98           C  
ANISOU 2015  CZ3 TRP A 265     2231   2055   2545   -132     24     -4       C  
ATOM   2016  CH2 TRP A 265      10.939  25.179  31.582  1.00 20.04           C  
ANISOU 2016  CH2 TRP A 265     2509   2323   2783   -129      4    -12       C  
ATOM   2017  N   LEU A 266      17.850  29.411  32.558  1.00 21.24           N  
ANISOU 2017  N   LEU A 266     2423   2456   3192   -170     29    -37       N  
ATOM   2018  CA  LEU A 266      18.561  30.482  31.851  1.00 19.77           C  
ANISOU 2018  CA  LEU A 266     2209   2245   3056   -186     64    -34       C  
ATOM   2019  C   LEU A 266      19.092  30.075  30.478  1.00 24.88           C  
ANISOU 2019  C   LEU A 266     2865   2880   3709   -173    112     -5       C  
ATOM   2020  O   LEU A 266      19.051  30.919  29.567  1.00 24.26           O  
ANISOU 2020  O   LEU A 266     2792   2778   3649   -181    151     11       O  
ATOM   2021  CB  LEU A 266      19.699  31.046  32.716  1.00 23.92           C  
ANISOU 2021  CB  LEU A 266     2675   2779   3636   -202     47    -64       C  
ATOM   2022  CG  LEU A 266      19.323  32.125  33.735  1.00 31.96           C  
ANISOU 2022  CG  LEU A 266     3678   3796   4670   -226     19    -97       C  
ATOM   2023  CD1 LEU A 266      20.561  32.563  34.537  1.00 32.31           C  
ANISOU 2023  CD1 LEU A 266     3657   3855   4767   -241      1   -134       C  
ATOM   2024  CD2 LEU A 266      18.714  33.329  33.035  1.00 31.82           C  
ANISOU 2024  CD2 LEU A 266     3677   3740   4671   -244     55    -88       C  
ATOM   2025  N   PRO A 267      19.658  28.879  30.262  1.00 20.49           N  
ANISOU 2025  N   PRO A 267     2307   2336   3141   -152    115      4       N  
ATOM   2026  CA  PRO A 267      20.048  28.533  28.878  1.00 20.00           C  
ANISOU 2026  CA  PRO A 267     2258   2262   3079   -139    164     30       C  
ATOM   2027  C   PRO A 267      18.870  28.620  27.922  1.00 22.52           C  
ANISOU 2027  C   PRO A 267     2630   2573   3352   -134    184     47       C  
ATOM   2028  O   PRO A 267      18.973  29.237  26.851  1.00 24.92           O  
ANISOU 2028  O   PRO A 267     2941   2862   3665   -133    226     67       O  
ATOM   2029  CB  PRO A 267      20.579  27.098  29.009  1.00 22.62           C  
ANISOU 2029  CB  PRO A 267     2589   2610   3398   -115    157     32       C  
ATOM   2030  CG  PRO A 267      21.008  26.985  30.493  1.00 26.60           C  
ANISOU 2030  CG  PRO A 267     3055   3136   3918   -117    110     10       C  
ATOM   2031  CD  PRO A 267      19.954  27.786  31.210  1.00 22.90           C  
ANISOU 2031  CD  PRO A 267     2601   2667   3432   -136     80     -6       C  
ATOM   2032  N   TYR A 268      17.728  28.062  28.324  1.00 20.81           N  
ANISOU 2032  N   TYR A 268     2449   2370   3089   -130    154     40       N  
ATOM   2033  CA  TYR A 268      16.532  28.138  27.484  1.00 21.25           C  
ANISOU 2033  CA  TYR A 268     2550   2426   3100   -125    165     51       C  
ATOM   2034  C   TYR A 268      16.107  29.592  27.270  1.00 25.16           C  
ANISOU 2034  C   TYR A 268     3044   2905   3609   -138    177     60       C  
ATOM   2035  O   TYR A 268      15.873  30.024  26.133  1.00 20.66           O  
ANISOU 2035  O   TYR A 268     2493   2330   3027   -130    213     82       O  
ATOM   2036  CB  TYR A 268      15.393  27.323  28.118  1.00 21.73           C  
ANISOU 2036  CB  TYR A 268     2640   2501   3117   -122    129     37       C  
ATOM   2037  CG  TYR A 268      14.176  27.293  27.205  1.00 23.27           C  
ANISOU 2037  CG  TYR A 268     2876   2701   3264   -117    139     44       C  
ATOM   2038  CD1 TYR A 268      14.160  26.513  26.064  1.00 21.61           C  
ANISOU 2038  CD1 TYR A 268     2688   2496   3025   -101    165     51       C  
ATOM   2039  CD2 TYR A 268      13.070  28.088  27.476  1.00 19.67           C  
ANISOU 2039  CD2 TYR A 268     2434   2247   2793   -126    122     42       C  
ATOM   2040  CE1 TYR A 268      13.049  26.497  25.213  1.00 23.46           C  
ANISOU 2040  CE1 TYR A 268     2957   2744   3214    -95    170     52       C  
ATOM   2041  CE2 TYR A 268      11.957  28.092  26.642  1.00 24.57           C  
ANISOU 2041  CE2 TYR A 268     3088   2879   3370   -119    128     49       C  
ATOM   2042  CZ  TYR A 268      11.962  27.296  25.510  1.00 23.26           C  
ANISOU 2042  CZ  TYR A 268     2942   2724   3174   -104    150     52       C  
ATOM   2043  OH  TYR A 268      10.864  27.305  24.691  1.00 21.78           O  
ANISOU 2043  OH  TYR A 268     2782   2554   2940    -95    151     54       O  
ATOM   2044  N   ALA A 269      16.045  30.379  28.352  1.00 21.38           N  
ANISOU 2044  N   ALA A 269     2543   2421   3158   -157    151     42       N  
ATOM   2045  CA  ALA A 269      15.606  31.771  28.228  1.00 21.14           C  
ANISOU 2045  CA  ALA A 269     2514   2372   3148   -170    166     49       C  
ATOM   2046  C   ALA A 269      16.541  32.561  27.322  1.00 24.40           C  
ANISOU 2046  C   ALA A 269     2905   2760   3605   -172    217     70       C  
ATOM   2047  O   ALA A 269      16.092  33.392  26.519  1.00 21.07           O  
ANISOU 2047  O   ALA A 269     2501   2323   3181   -167    250     95       O  
ATOM   2048  CB  ALA A 269      15.545  32.430  29.611  1.00 21.70           C  
ANISOU 2048  CB  ALA A 269     2559   2439   3246   -191    131     19       C  
ATOM   2049  N   GLY A 270      17.852  32.347  27.470  1.00 22.76           N  
ANISOU 2049  N   GLY A 270     2659   2549   3441   -177    227     62       N  
ATOM   2050  CA  GLY A 270      18.805  33.089  26.653  1.00 24.54           C  
ANISOU 2050  CA  GLY A 270     2860   2748   3716   -180    280     82       C  
ATOM   2051  C   GLY A 270      18.737  32.723  25.178  1.00 24.00           C  
ANISOU 2051  C   GLY A 270     2824   2682   3614   -154    326    119       C  
ATOM   2052  O   GLY A 270      18.806  33.599  24.305  1.00 23.43           O  
ANISOU 2052  O   GLY A 270     2756   2588   3558   -150    374    148       O  
ATOM   2053  N   VAL A 271      18.606  31.434  24.872  1.00 20.30           N  
ANISOU 2053  N   VAL A 271     2378   2238   3098   -135    314    118       N  
ATOM   2054  CA  VAL A 271      18.541  31.044  23.465  1.00 21.83           C  
ANISOU 2054  CA  VAL A 271     2601   2438   3254   -110    355    147       C  
ATOM   2055  C   VAL A 271      17.242  31.539  22.843  1.00 21.07           C  
ANISOU 2055  C   VAL A 271     2548   2349   3108    -99    359    165       C  
ATOM   2056  O   VAL A 271      17.226  32.046  21.714  1.00 24.52           O  
ANISOU 2056  O   VAL A 271     3001   2783   3534    -81    404    197       O  
ATOM   2057  CB  VAL A 271      18.695  29.522  23.313  1.00 23.65           C  
ANISOU 2057  CB  VAL A 271     2847   2692   3450    -94    342    135       C  
ATOM   2058  CG1 VAL A 271      18.417  29.093  21.846  1.00 22.56           C  
ANISOU 2058  CG1 VAL A 271     2747   2566   3261    -68    380    157       C  
ATOM   2059  CG2 VAL A 271      20.098  29.092  23.772  1.00 25.34           C  
ANISOU 2059  CG2 VAL A 271     3015   2898   3714    -98    346    126       C  
ATOM   2060  N   ALA A 272      16.145  31.415  23.581  1.00 19.94           N  
ANISOU 2060  N   ALA A 272     2422   2219   2936   -106    313    146       N  
ATOM   2061  CA  ALA A 272      14.865  31.935  23.114  1.00 25.15           C  
ANISOU 2061  CA  ALA A 272     3116   2888   3551    -95    312    161       C  
ATOM   2062  C   ALA A 272      14.967  33.418  22.795  1.00 27.15           C  
ANISOU 2062  C   ALA A 272     3360   3113   3841    -97    350    189       C  
ATOM   2063  O   ALA A 272      14.529  33.865  21.726  1.00 23.38           O  
ANISOU 2063  O   ALA A 272     2907   2641   3335    -74    382    223       O  
ATOM   2064  CB  ALA A 272      13.781  31.685  24.174  1.00 21.97           C  
ANISOU 2064  CB  ALA A 272     2724   2498   3127   -107    257    134       C  
ATOM   2065  N   PHE A 273      15.524  34.206  23.729  1.00 22.45           N  
ANISOU 2065  N   PHE A 273     2729   2489   3312   -123    346    176       N  
ATOM   2066  CA  PHE A 273      15.638  35.646  23.498  1.00 24.70           C  
ANISOU 2066  CA  PHE A 273     3004   2739   3643   -128    387    200       C  
ATOM   2067  C   PHE A 273      16.570  35.943  22.334  1.00 25.74           C  
ANISOU 2067  C   PHE A 273     3129   2854   3797   -113    452    236       C  
ATOM   2068  O   PHE A 273      16.332  36.878  21.562  1.00 25.54           O  
ANISOU 2068  O   PHE A 273     3117   2811   3777    -98    498    275       O  
ATOM   2069  CB  PHE A 273      16.123  36.382  24.746  1.00 25.44           C  
ANISOU 2069  CB  PHE A 273     3056   2803   3805   -163    371    168       C  
ATOM   2070  CG  PHE A 273      15.982  37.895  24.634  1.00 30.36           C  
ANISOU 2070  CG  PHE A 273     3672   3385   4477   -171    411    187       C  
ATOM   2071  CD1 PHE A 273      14.723  38.476  24.644  1.00 38.68           C  
ANISOU 2071  CD1 PHE A 273     4756   4438   5501   -161    404    200       C  
ATOM   2072  CD2 PHE A 273      17.089  38.713  24.456  1.00 36.14           C  
ANISOU 2072  CD2 PHE A 273     4368   4076   5285   -186    461    194       C  
ATOM   2073  CE1 PHE A 273      14.562  39.849  24.522  1.00 44.87           C  
ANISOU 2073  CE1 PHE A 273     5537   5181   6331   -164    445    220       C  
ATOM   2074  CE2 PHE A 273      16.943  40.117  24.329  1.00 28.52           C  
ANISOU 2074  CE2 PHE A 273     3399   3066   4372   -194    505    213       C  
ATOM   2075  CZ  PHE A 273      15.669  40.672  24.366  1.00 36.45           C  
ANISOU 2075  CZ  PHE A 273     4436   4069   5344   -181    498    227       C  
ATOM   2076  N   TYR A 274      17.653  35.180  22.200  1.00 22.36           N  
ANISOU 2076  N   TYR A 274     2680   2431   3386   -115    461    228       N  
ATOM   2077  CA  TYR A 274      18.504  35.358  21.026  1.00 22.18           C  
ANISOU 2077  CA  TYR A 274     2654   2396   3379    -98    526    264       C  
ATOM   2078  C   TYR A 274      17.717  35.136  19.738  1.00 25.37           C  
ANISOU 2078  C   TYR A 274     3106   2826   3706    -59    549    300       C  
ATOM   2079  O   TYR A 274      17.808  35.926  18.784  1.00 25.72           O  
ANISOU 2079  O   TYR A 274     3162   2857   3754    -39    606    345       O  
ATOM   2080  CB  TYR A 274      19.698  34.399  21.096  1.00 26.48           C  
ANISOU 2080  CB  TYR A 274     3170   2948   3945   -102    527    246       C  
ATOM   2081  CG  TYR A 274      20.577  34.524  19.875  1.00 26.09           C  
ANISOU 2081  CG  TYR A 274     3117   2886   3909    -82    597    284       C  
ATOM   2082  CD1 TYR A 274      21.566  35.502  19.811  1.00 34.80           C  
ANISOU 2082  CD1 TYR A 274     4181   3949   5094    -98    648    298       C  
ATOM   2083  CD2 TYR A 274      20.412  33.684  18.781  1.00 29.44           C  
ANISOU 2083  CD2 TYR A 274     3578   3341   4268    -49    615    302       C  
ATOM   2084  CE1 TYR A 274      22.369  35.629  18.702  1.00 34.23           C  
ANISOU 2084  CE1 TYR A 274     4105   3864   5036    -80    717    335       C  
ATOM   2085  CE2 TYR A 274      21.216  33.813  17.664  1.00 36.33           C  
ANISOU 2085  CE2 TYR A 274     4449   4204   5150    -29    682    338       C  
ATOM   2086  CZ  TYR A 274      22.185  34.796  17.638  1.00 40.56           C  
ANISOU 2086  CZ  TYR A 274     4946   4698   5767    -43    733    357       C  
ATOM   2087  OH  TYR A 274      23.000  34.947  16.543  1.00 46.44           O  
ANISOU 2087  OH  TYR A 274     5688   5432   6525    -23    805    395       O  
ATOM   2088  N   ILE A 275      16.935  34.058  19.690  1.00 24.62           N  
ANISOU 2088  N   ILE A 275     3042   2772   3541    -46    506    282       N  
ATOM   2089  CA  ILE A 275      16.210  33.739  18.460  1.00 22.93           C  
ANISOU 2089  CA  ILE A 275     2870   2592   3249    -10    522    307       C  
ATOM   2090  C   ILE A 275      15.232  34.854  18.145  1.00 22.76           C  
ANISOU 2090  C   ILE A 275     2869   2569   3209      5    534    339       C  
ATOM   2091  O   ILE A 275      15.194  35.381  17.020  1.00 25.21           O  
ANISOU 2091  O   ILE A 275     3198   2884   3496     37    583    384       O  
ATOM   2092  CB  ILE A 275      15.502  32.377  18.603  1.00 24.05           C  
ANISOU 2092  CB  ILE A 275     3036   2775   3328     -6    471    271       C  
ATOM   2093  CG1 ILE A 275      16.550  31.248  18.569  1.00 27.04           C  
ANISOU 2093  CG1 ILE A 275     3400   3154   3719     -9    476    251       C  
ATOM   2094  CG2 ILE A 275      14.491  32.164  17.476  1.00 27.56           C  
ANISOU 2094  CG2 ILE A 275     3522   3260   3689     27    475    286       C  
ATOM   2095  CD1 ILE A 275      15.952  29.851  18.890  1.00 30.08           C  
ANISOU 2095  CD1 ILE A 275     3803   3568   4057    -11    429    211       C  
ATOM   2096  N   PHE A 276      14.495  35.287  19.173  1.00 22.30           N  
ANISOU 2096  N   PHE A 276     2805   2500   3166    -16    494    319       N  
ATOM   2097  CA  PHE A 276      13.488  36.333  19.009  1.00 26.35           C  
ANISOU 2097  CA  PHE A 276     3336   3010   3666     -1    501    347       C  
ATOM   2098  C   PHE A 276      14.083  37.610  18.415  1.00 26.83           C  
ANISOU 2098  C   PHE A 276     3388   3031   3776     10    572    396       C  
ATOM   2099  O   PHE A 276      13.411  38.327  17.661  1.00 28.79           O  
ANISOU 2099  O   PHE A 276     3660   3285   3995     42    600    440       O  
ATOM   2100  CB  PHE A 276      12.851  36.618  20.370  1.00 23.62           C  
ANISOU 2100  CB  PHE A 276     2978   2650   3346    -31    452    313       C  
ATOM   2101  CG  PHE A 276      11.807  37.696  20.341  1.00 24.49           C  
ANISOU 2101  CG  PHE A 276     3103   2753   3449    -18    458    339       C  
ATOM   2102  CD1 PHE A 276      10.645  37.530  19.609  1.00 25.30           C  
ANISOU 2102  CD1 PHE A 276     3238   2897   3476     16    446    358       C  
ATOM   2103  CD2 PHE A 276      11.974  38.852  21.085  1.00 32.32           C  
ANISOU 2103  CD2 PHE A 276     4073   3697   4511    -40    473    339       C  
ATOM   2104  CE1 PHE A 276       9.672  38.529  19.587  1.00 34.52           C  
ANISOU 2104  CE1 PHE A 276     4418   4060   4638     32    452    384       C  
ATOM   2105  CE2 PHE A 276      11.008  39.849  21.078  1.00 33.54           C  
ANISOU 2105  CE2 PHE A 276     4241   3840   4662    -26    482    364       C  
ATOM   2106  CZ  PHE A 276       9.863  39.690  20.318  1.00 35.30           C  
ANISOU 2106  CZ  PHE A 276     4497   4105   4809     12    472    390       C  
ATOM   2107  N   THR A 277      15.329  37.928  18.763  1.00 24.62           N  
ANISOU 2107  N   THR A 277     3072   2709   3575    -16    602    391       N  
ATOM   2108  CA  THR A 277      15.970  39.147  18.284  1.00 24.13           C  
ANISOU 2108  CA  THR A 277     2995   2599   3573    -11    674    434       C  
ATOM   2109  C   THR A 277      16.819  38.905  17.046  1.00 31.21           C  
ANISOU 2109  C   THR A 277     3897   3502   4459     16    734    472       C  
ATOM   2110  O   THR A 277      17.450  39.845  16.544  1.00 33.87           O  
ANISOU 2110  O   THR A 277     4223   3798   4848     22    804    513       O  
ATOM   2111  CB  THR A 277      16.843  39.778  19.402  1.00 28.03           C  
ANISOU 2111  CB  THR A 277     3439   3040   4169    -59    677    402       C  
ATOM   2112  OG1 THR A 277      17.751  38.810  19.903  1.00 26.61           O  
ANISOU 2112  OG1 THR A 277     3230   2872   4007    -81    649    360       O  
ATOM   2113  CG2 THR A 277      15.970  40.243  20.576  1.00 29.66           C  
ANISOU 2113  CG2 THR A 277     3642   3237   4388    -82    628    369       C  
ATOM   2114  N   HIS A 278      16.866  37.665  16.562  1.00 23.69           N  
ANISOU 2114  N   HIS A 278     2963   2596   3444     32    713    458       N  
ATOM   2115  CA  HIS A 278      17.683  37.273  15.407  1.00 25.94           C  
ANISOU 2115  CA  HIS A 278     3255   2892   3711     59    766    488       C  
ATOM   2116  C   HIS A 278      16.880  36.324  14.527  1.00 30.93           C  
ANISOU 2116  C   HIS A 278     3930   3587   4234     96    744    489       C  
ATOM   2117  O   HIS A 278      17.360  35.274  14.106  1.00 29.01           O  
ANISOU 2117  O   HIS A 278     3692   3369   3962    104    742    472       O  
ATOM   2118  CB  HIS A 278      19.001  36.617  15.832  1.00 27.97           C  
ANISOU 2118  CB  HIS A 278     3472   3132   4024     31    769    456       C  
ATOM   2119  CG  HIS A 278      19.902  37.538  16.581  1.00 33.06           C  
ANISOU 2119  CG  HIS A 278     4067   3719   4774     -6    794    451       C  
ATOM   2120  ND1 HIS A 278      19.693  37.859  17.903  1.00 30.13           N  
ANISOU 2120  ND1 HIS A 278     3670   3328   4449    -44    746    410       N  
ATOM   2121  CD2 HIS A 278      20.982  38.254  16.179  1.00 32.54           C  
ANISOU 2121  CD2 HIS A 278     3973   3611   4780    -10    865    480       C  
ATOM   2122  CE1 HIS A 278      20.618  38.718  18.295  1.00 36.27           C  
ANISOU 2122  CE1 HIS A 278     4403   4056   5321    -72    783    408       C  
ATOM   2123  NE2 HIS A 278      21.413  38.970  17.271  1.00 36.46           N  
ANISOU 2123  NE2 HIS A 278     4423   4063   5366    -54    856    450       N  
ATOM   2124  N   GLN A 279      15.626  36.677  14.273  1.00 28.16           N  
ANISOU 2124  N   GLN A 279     3610   3263   3826    120    725    505       N  
ATOM   2125  CA  GLN A 279      14.737  35.785  13.538  1.00 33.46           C  
ANISOU 2125  CA  GLN A 279     4319   4000   4396    151    694    495       C  
ATOM   2126  C   GLN A 279      15.276  35.518  12.143  1.00 31.46           C  
ANISOU 2126  C   GLN A 279     4086   3773   4096    192    749    529       C  
ATOM   2127  O   GLN A 279      15.758  36.428  11.468  1.00 28.78           O  
ANISOU 2127  O   GLN A 279     3747   3411   3777    216    816    585       O  
ATOM   2128  CB  GLN A 279      13.334  36.385  13.447  1.00 30.66           C  
ANISOU 2128  CB  GLN A 279     3988   3671   3992    173    670    513       C  
ATOM   2129  CG  GLN A 279      12.558  36.241  14.749  1.00 27.46           C  
ANISOU 2129  CG  GLN A 279     3571   3259   3604    137    602    467       C  
ATOM   2130  CD  GLN A 279      11.186  36.867  14.708  1.00 31.60           C  
ANISOU 2130  CD  GLN A 279     4113   3805   4087    158    580    485       C  
ATOM   2131  OE1 GLN A 279      10.855  37.602  13.785  1.00 36.33           O  
ANISOU 2131  OE1 GLN A 279     4732   4419   4654    201    618    538       O  
ATOM   2132  NE2 GLN A 279      10.379  36.588  15.725  1.00 30.41           N  
ANISOU 2132  NE2 GLN A 279     3957   3660   3938    132    519    443       N  
ATOM   2133  N   GLY A 280      15.203  34.257  11.715  1.00 32.23           N  
ANISOU 2133  N   GLY A 280     4200   3916   4132    201    723    495       N  
ATOM   2134  CA  GLY A 280      15.635  33.891  10.381  1.00 38.16           C  
ANISOU 2134  CA  GLY A 280     4973   4699   4827    241    771    519       C  
ATOM   2135  C   GLY A 280      17.128  33.742  10.210  1.00 36.52           C  
ANISOU 2135  C   GLY A 280     4742   4454   4678    233    826    529       C  
ATOM   2136  O   GLY A 280      17.588  33.455   9.093  1.00 35.43           O  
ANISOU 2136  O   GLY A 280     4623   4341   4498    267    872    550       O  
ATOM   2137  N   SER A 281      17.906  33.932  11.269  1.00 32.26           N  
ANISOU 2137  N   SER A 281     4162   3862   4233    189    822    512       N  
ATOM   2138  CA  SER A 281      19.347  33.809  11.149  1.00 30.43           C  
ANISOU 2138  CA  SER A 281     3902   3597   4064    180    872    520       C  
ATOM   2139  C   SER A 281      19.742  32.335  11.107  1.00 33.75           C  
ANISOU 2139  C   SER A 281     4325   4043   4458    176    848    473       C  
ATOM   2140  O   SER A 281      18.921  31.427  11.266  1.00 30.51           O  
ANISOU 2140  O   SER A 281     3936   3669   3989    175    792    432       O  
ATOM   2141  CB  SER A 281      20.039  34.533  12.307  1.00 35.35           C  
ANISOU 2141  CB  SER A 281     4476   4159   4797    135    873    513       C  
ATOM   2142  OG  SER A 281      19.690  33.922  13.537  1.00 32.53           O  
ANISOU 2142  OG  SER A 281     4104   3804   4453     99    798    457       O  
ATOM   2143  N   ASP A 282      21.022  32.103  10.894  1.00 31.28           N  
ANISOU 2143  N   ASP A 282     3987   3706   4192    173    894    480       N  
ATOM   2144  CA  ASP A 282      21.522  30.761  10.614  1.00 37.04           C  
ANISOU 2144  CA  ASP A 282     4722   4457   4896    179    889    446       C  
ATOM   2145  C   ASP A 282      21.782  30.042  11.929  1.00 38.71           C  
ANISOU 2145  C   ASP A 282     4900   4650   5159    139    833    395       C  
ATOM   2146  O   ASP A 282      22.841  30.201  12.539  1.00 43.28           O  
ANISOU 2146  O   ASP A 282     5434   5192   5818    116    847    394       O  
ATOM   2147  CB  ASP A 282      22.787  30.837   9.766  1.00 32.98           C  
ANISOU 2147  CB  ASP A 282     4194   3926   4409    198    968    479       C  
ATOM   2148  CG  ASP A 282      23.185  29.494   9.203  1.00 47.71           C  
ANISOU 2148  CG  ASP A 282     6075   5820   6233    215    974    450       C  
ATOM   2149  OD1 ASP A 282      22.361  28.550   9.264  1.00 49.95           O  
ANISOU 2149  OD1 ASP A 282     6385   6138   6454    217    922    407       O  
ATOM   2150  OD2 ASP A 282      24.324  29.388   8.705  1.00 55.94           O  
ANISOU 2150  OD2 ASP A 282     7100   6847   7309    226   1033    468       O  
ATOM   2151  N   PHE A 283      20.812  29.254  12.385  1.00 30.99           N  
ANISOU 2151  N   PHE A 283     3943   3698   4133    131    769    354       N  
ATOM   2152  CA  PHE A 283      21.035  28.336  13.487  1.00 32.08           C  
ANISOU 2152  CA  PHE A 283     4058   3826   4305    103    720    308       C  
ATOM   2153  C   PHE A 283      20.422  27.002  13.090  1.00 31.79           C  
ANISOU 2153  C   PHE A 283     4056   3825   4197    116    695    271       C  
ATOM   2154  O   PHE A 283      19.549  26.930  12.223  1.00 29.43           O  
ANISOU 2154  O   PHE A 283     3797   3563   3822    139    695    272       O  
ATOM   2155  CB  PHE A 283      20.458  28.844  14.815  1.00 30.67           C  
ANISOU 2155  CB  PHE A 283     3861   3631   4162     70    664    293       C  
ATOM   2156  CG  PHE A 283      18.995  29.218  14.752  1.00 27.82           C  
ANISOU 2156  CG  PHE A 283     3533   3294   3742     75    630    292       C  
ATOM   2157  CD1 PHE A 283      18.016  28.268  14.970  1.00 32.02           C  
ANISOU 2157  CD1 PHE A 283     4090   3855   4220     73    580    254       C  
ATOM   2158  CD2 PHE A 283      18.615  30.530  14.522  1.00 28.99           C  
ANISOU 2158  CD2 PHE A 283     3685   3434   3896     81    651    330       C  
ATOM   2159  CE1 PHE A 283      16.672  28.613  14.917  1.00 29.98           C  
ANISOU 2159  CE1 PHE A 283     3858   3622   3911     78    548    253       C  
ATOM   2160  CE2 PHE A 283      17.271  30.893  14.472  1.00 29.24           C  
ANISOU 2160  CE2 PHE A 283     3744   3489   3875     89    620    332       C  
ATOM   2161  CZ  PHE A 283      16.302  29.939  14.655  1.00 26.52           C  
ANISOU 2161  CZ  PHE A 283     3423   3179   3475     88    567    293       C  
ATOM   2162  N   GLY A 284      20.935  25.942  13.686  1.00 27.83           N  
ANISOU 2162  N   GLY A 284     3539   3313   3722    104    676    238       N  
ATOM   2163  CA  GLY A 284      20.531  24.613  13.306  1.00 28.74           C  
ANISOU 2163  CA  GLY A 284     3684   3452   3783    115    663    201       C  
ATOM   2164  C   GLY A 284      19.600  24.021  14.346  1.00 24.91           C  
ANISOU 2164  C   GLY A 284     3204   2970   3292     92    598    163       C  
ATOM   2165  O   GLY A 284      19.210  24.671  15.319  1.00 26.72           O  
ANISOU 2165  O   GLY A 284     3416   3186   3549     70    562    167       O  
ATOM   2166  N   PRO A 285      19.252  22.748  14.159  1.00 24.43           N  
ANISOU 2166  N   PRO A 285     3166   2922   3196     96    585    124       N  
ATOM   2167  CA  PRO A 285      18.305  22.085  15.075  1.00 25.20           C  
ANISOU 2167  CA  PRO A 285     3270   3019   3285     76    530     88       C  
ATOM   2168  C   PRO A 285      18.857  21.811  16.463  1.00 22.50           C  
ANISOU 2168  C   PRO A 285     2894   2645   3009     56    505     84       C  
ATOM   2169  O   PRO A 285      18.077  21.735  17.415  1.00 22.90           O  
ANISOU 2169  O   PRO A 285     2945   2694   3062     38    459     69       O  
ATOM   2170  CB  PRO A 285      17.984  20.756  14.361  1.00 26.04           C  
ANISOU 2170  CB  PRO A 285     3408   3142   3346     88    538     47       C  
ATOM   2171  CG  PRO A 285      18.595  20.840  13.043  1.00 31.62           C  
ANISOU 2171  CG  PRO A 285     4127   3865   4024    115    592     61       C  
ATOM   2172  CD  PRO A 285      19.597  21.928  12.987  1.00 25.09           C  
ANISOU 2172  CD  PRO A 285     3273   3022   3240    122    626    111       C  
ATOM   2173  N   ILE A 286      20.164  21.595  16.612  1.00 24.32           N  
ANISOU 2173  N   ILE A 286     3096   2855   3291     62    533     97       N  
ATOM   2174  CA  ILE A 286      20.682  21.273  17.935  1.00 27.61           C  
ANISOU 2174  CA  ILE A 286     3478   3249   3763     48    505     92       C  
ATOM   2175  C   ILE A 286      20.679  22.492  18.850  1.00 22.06           C  
ANISOU 2175  C   ILE A 286     2746   2540   3097     28    478    110       C  
ATOM   2176  O   ILE A 286      20.658  22.352  20.079  1.00 23.76           O  
ANISOU 2176  O   ILE A 286     2940   2747   3340     15    439    100       O  
ATOM   2177  CB  ILE A 286      22.098  20.676  17.793  1.00 27.73           C  
ANISOU 2177  CB  ILE A 286     3466   3248   3821     64    543    100       C  
ATOM   2178  CG1 ILE A 286      22.054  19.452  16.878  1.00 35.26           C  
ANISOU 2178  CG1 ILE A 286     4452   4206   4737     84    573     78       C  
ATOM   2179  CG2 ILE A 286      22.651  20.258  19.152  1.00 29.80           C  
ANISOU 2179  CG2 ILE A 286     3692   3495   4136     56    513     96       C  
ATOM   2180  CD1 ILE A 286      21.114  18.362  17.398  1.00 36.83           C  
ANISOU 2180  CD1 ILE A 286     4678   4404   4914     77    539     43       C  
ATOM   2181  N   PHE A 287      20.703  23.690  18.272  1.00 21.25           N  
ANISOU 2181  N   PHE A 287     2641   2440   2995     28    501    135       N  
ATOM   2182  CA  PHE A 287      20.826  24.929  19.041  1.00 23.22           C  
ANISOU 2182  CA  PHE A 287     2858   2675   3288      8    485    150       C  
ATOM   2183  C   PHE A 287      19.771  25.037  20.145  1.00 26.86           C  
ANISOU 2183  C   PHE A 287     3326   3141   3739    -11    427    132       C  
ATOM   2184  O   PHE A 287      20.099  25.273  21.318  1.00 23.59           O  
ANISOU 2184  O   PHE A 287     2879   2716   3367    -28    397    124       O  
ATOM   2185  CB  PHE A 287      20.721  26.095  18.056  1.00 24.00           C  
ANISOU 2185  CB  PHE A 287     2968   2776   3377     16    524    182       C  
ATOM   2186  CG  PHE A 287      20.921  27.462  18.654  1.00 22.77           C  
ANISOU 2186  CG  PHE A 287     2781   2599   3272     -4    523    199       C  
ATOM   2187  CD1 PHE A 287      22.068  27.785  19.358  1.00 31.44           C  
ANISOU 2187  CD1 PHE A 287     3828   3675   4444    -20    528    199       C  
ATOM   2188  CD2 PHE A 287      19.990  28.457  18.402  1.00 25.06           C  
ANISOU 2188  CD2 PHE A 287     3092   2892   3539     -5    522    216       C  
ATOM   2189  CE1 PHE A 287      22.245  29.077  19.865  1.00 37.52           C  
ANISOU 2189  CE1 PHE A 287     4568   4423   5266    -42    531    208       C  
ATOM   2190  CE2 PHE A 287      20.158  29.734  18.892  1.00 26.64           C  
ANISOU 2190  CE2 PHE A 287     3265   3067   3790    -23    527    230       C  
ATOM   2191  CZ  PHE A 287      21.285  30.055  19.624  1.00 32.24           C  
ANISOU 2191  CZ  PHE A 287     3923   3752   4575    -44    532    224       C  
ATOM   2192  N   MET A 288      18.497  24.861  19.794  1.00 21.41           N  
ANISOU 2192  N   MET A 288     2676   2470   2990     -8    409    121       N  
ATOM   2193  CA  MET A 288      17.468  24.921  20.823  1.00 20.14           C  
ANISOU 2193  CA  MET A 288     2521   2312   2820    -26    357    104       C  
ATOM   2194  C   MET A 288      17.183  23.561  21.448  1.00 21.11           C  
ANISOU 2194  C   MET A 288     2653   2436   2930    -26    330     75       C  
ATOM   2195  O   MET A 288      16.632  23.521  22.543  1.00 22.37           O  
ANISOU 2195  O   MET A 288     2808   2594   3096    -40    290     63       O  
ATOM   2196  CB  MET A 288      16.169  25.534  20.258  1.00 21.81           C  
ANISOU 2196  CB  MET A 288     2764   2542   2980    -24    349    108       C  
ATOM   2197  CG  MET A 288      15.057  25.771  21.329  1.00 19.67           C  
ANISOU 2197  CG  MET A 288     2497   2274   2702    -42    299     92       C  
ATOM   2198  SD  MET A 288      15.570  26.597  22.866  1.00 23.69           S  
ANISOU 2198  SD  MET A 288     2965   2760   3276    -65    272     94       S  
ATOM   2199  CE  MET A 288      14.759  28.197  22.702  1.00 23.73           C  
ANISOU 2199  CE  MET A 288     2977   2763   3278    -71    274    114       C  
ATOM   2200  N   THR A 289      17.547  22.449  20.798  1.00 20.13           N  
ANISOU 2200  N   THR A 289     2542   2314   2793    -11    354     65       N  
ATOM   2201  CA  THR A 289      17.201  21.143  21.367  1.00 19.99           C  
ANISOU 2201  CA  THR A 289     2537   2292   2768    -12    335     39       C  
ATOM   2202  C   THR A 289      17.789  20.953  22.767  1.00 22.53           C  
ANISOU 2202  C   THR A 289     2826   2599   3135    -17    309     42       C  
ATOM   2203  O   THR A 289      17.087  20.550  23.697  1.00 19.62           O  
ANISOU 2203  O   THR A 289     2465   2230   2762    -25    276     29       O  
ATOM   2204  CB  THR A 289      17.669  20.006  20.446  1.00 21.26           C  
ANISOU 2204  CB  THR A 289     2712   2449   2915      7    372     27       C  
ATOM   2205  OG1 THR A 289      16.943  20.088  19.224  1.00 20.89           O  
ANISOU 2205  OG1 THR A 289     2699   2425   2815     13    388     16       O  
ATOM   2206  CG2 THR A 289      17.358  18.655  21.078  1.00 24.60           C  
ANISOU 2206  CG2 THR A 289     3147   2860   3341      6    359      2       C  
ATOM   2207  N  AILE A 290      19.085  21.220  22.933  0.65 20.08           N  
ANISOU 2207  N  AILE A 290     2479   2281   2871    -11    326     58       N  
ATOM   2208  N  BILE A 290      19.084  21.227  22.931  0.35 20.08           N  
ANISOU 2208  N  BILE A 290     2479   2281   2871    -11    326     58       N  
ATOM   2209  CA AILE A 290      19.726  20.949  24.221  0.65 21.32           C  
ANISOU 2209  CA AILE A 290     2602   2432   3067    -10    300     60       C  
ATOM   2210  CA BILE A 290      19.737  20.953  24.213  0.35 21.38           C  
ANISOU 2210  CA BILE A 290     2609   2440   3074    -10    301     60       C  
ATOM   2211  C  AILE A 290      19.128  21.781  25.348  0.65 19.78           C  
ANISOU 2211  C  AILE A 290     2396   2244   2876    -30    255     56       C  
ATOM   2212  C  BILE A 290      19.150  21.782  25.351  0.35 19.79           C  
ANISOU 2212  C  BILE A 290     2396   2245   2878    -29    255     56       C  
ATOM   2213  O  AILE A 290      18.725  21.197  26.366  0.65 20.00           O  
ANISOU 2213  O  AILE A 290     2426   2274   2899    -29    224     48       O  
ATOM   2214  O  BILE A 290      18.782  21.196  26.382  0.35 20.06           O  
ANISOU 2214  O  BILE A 290     2432   2281   2908    -28    224     48       O  
ATOM   2215  CB AILE A 290      21.252  21.112  24.104  0.65 24.11           C  
ANISOU 2215  CB AILE A 290     2912   2780   3468      0    326     75       C  
ATOM   2216  CB BILE A 290      21.262  21.112  24.077  0.35 24.07           C  
ANISOU 2216  CB BILE A 290     2907   2775   3463      0    328     75       C  
ATOM   2217  CG1AILE A 290      21.766  20.264  22.941  0.65 26.53           C  
ANISOU 2217  CG1AILE A 290     3234   3079   3767     21    375     78       C  
ATOM   2218  CG1BILE A 290      21.800  20.059  23.101  0.35 26.23           C  
ANISOU 2218  CG1BILE A 290     3195   3041   3731     23    372     76       C  
ATOM   2219  CG2AILE A 290      21.912  20.696  25.438  0.65 24.46           C  
ANISOU 2219  CG2AILE A 290     2919   2827   3546      6    296     75       C  
ATOM   2220  CG2BILE A 290      21.926  20.996  25.451  0.35 25.14           C  
ANISOU 2220  CG2BILE A 290     3001   2914   3636      2    294     75       C  
ATOM   2221  CD1AILE A 290      21.437  18.802  23.087  0.65 27.89           C  
ANISOU 2221  CD1AILE A 290     3431   3244   3920     35    375     63       C  
ATOM   2222  CD1BILE A 290      23.273  20.185  22.792  0.35 24.41           C  
ANISOU 2222  CD1BILE A 290     2924   2804   3547     35    406     92       C  
ATOM   2223  N   PRO A 291      19.027  23.112  25.247  1.00 19.76           N  
ANISOU 2223  N   PRO A 291     2382   2243   2883    -45    253     63       N  
ATOM   2224  CA  PRO A 291      18.409  23.849  26.356  1.00 19.52           C  
ANISOU 2224  CA  PRO A 291     2344   2218   2857    -63    211     55       C  
ATOM   2225  C   PRO A 291      16.959  23.468  26.587  1.00 19.20           C  
ANISOU 2225  C   PRO A 291     2342   2183   2770    -68    186     43       C  
ATOM   2226  O   PRO A 291      16.523  23.446  27.737  1.00 19.63           O  
ANISOU 2226  O   PRO A 291     2392   2243   2824    -74    150     34       O  
ATOM   2227  CB  PRO A 291      18.512  25.323  25.928  1.00 22.38           C  
ANISOU 2227  CB  PRO A 291     2692   2574   3239    -78    226     66       C  
ATOM   2228  CG  PRO A 291      19.385  25.365  24.753  1.00 28.88           C  
ANISOU 2228  CG  PRO A 291     3510   3389   4076    -66    275     83       C  
ATOM   2229  CD  PRO A 291      19.466  24.013  24.155  1.00 19.99           C  
ANISOU 2229  CD  PRO A 291     2406   2267   2923    -46    292     80       C  
ATOM   2230  N   ALA A 292      16.204  23.178  25.520  1.00 19.17           N  
ANISOU 2230  N   ALA A 292     2374   2182   2727    -63    205     41       N  
ATOM   2231  CA  ALA A 292      14.779  22.864  25.697  1.00 18.90           C  
ANISOU 2231  CA  ALA A 292     2372   2156   2654    -70    182     26       C  
ATOM   2232  C   ALA A 292      14.605  21.555  26.440  1.00 20.95           C  
ANISOU 2232  C   ALA A 292     2639   2410   2910    -65    168     12       C  
ATOM   2233  O   ALA A 292      13.698  21.418  27.266  1.00 22.00           O  
ANISOU 2233  O   ALA A 292     2783   2546   3031    -73    140      3       O  
ATOM   2234  CB  ALA A 292      14.056  22.798  24.345  1.00 22.69           C  
ANISOU 2234  CB  ALA A 292     2884   2647   3090    -65    203     22       C  
ATOM   2235  N   PHE A 293      15.447  20.559  26.135  1.00 19.04           N  
ANISOU 2235  N   PHE A 293     2395   2160   2682    -49    192     13       N  
ATOM   2236  CA  PHE A 293      15.340  19.293  26.861  1.00 19.04           C  
ANISOU 2236  CA  PHE A 293     2401   2148   2684    -40    186      6       C  
ATOM   2237  C   PHE A 293      16.013  19.342  28.228  1.00 20.48           C  
ANISOU 2237  C   PHE A 293     2553   2333   2896    -33    162     18       C  
ATOM   2238  O   PHE A 293      15.531  18.705  29.178  1.00 18.95           O  
ANISOU 2238  O   PHE A 293     2367   2137   2698    -29    144     17       O  
ATOM   2239  CB  PHE A 293      15.914  18.154  25.985  1.00 20.29           C  
ANISOU 2239  CB  PHE A 293     2571   2294   2845    -23    226      1       C  
ATOM   2240  CG  PHE A 293      14.864  17.585  25.061  1.00 20.19           C  
ANISOU 2240  CG  PHE A 293     2595   2281   2795    -30    239    -24       C  
ATOM   2241  CD1 PHE A 293      14.451  18.302  23.961  1.00 20.21           C  
ANISOU 2241  CD1 PHE A 293     2610   2300   2767    -37    248    -30       C  
ATOM   2242  CD2 PHE A 293      14.211  16.393  25.372  1.00 20.65           C  
ANISOU 2242  CD2 PHE A 293     2675   2324   2849    -31    241    -43       C  
ATOM   2243  CE1 PHE A 293      13.413  17.838  23.147  1.00 23.41           C  
ANISOU 2243  CE1 PHE A 293     3047   2715   3134    -43    253    -58       C  
ATOM   2244  CE2 PHE A 293      13.205  15.897  24.544  1.00 20.76           C  
ANISOU 2244  CE2 PHE A 293     2718   2340   2831    -41    251    -74       C  
ATOM   2245  CZ  PHE A 293      12.799  16.621  23.447  1.00 22.93           C  
ANISOU 2245  CZ  PHE A 293     3002   2639   3071    -48    253    -84       C  
ATOM   2246  N   PHE A 294      17.116  20.080  28.367  1.00 20.22           N  
ANISOU 2246  N   PHE A 294     2483   2306   2894    -31    161     30       N  
ATOM   2247  CA  PHE A 294      17.687  20.248  29.706  1.00 21.26           C  
ANISOU 2247  CA  PHE A 294     2581   2448   3048    -25    130     36       C  
ATOM   2248  C   PHE A 294      16.657  20.837  30.668  1.00 20.78           C  
ANISOU 2248  C   PHE A 294     2529   2398   2968    -40     92     28       C  
ATOM   2249  O   PHE A 294      16.565  20.434  31.838  1.00 20.76           O  
ANISOU 2249  O   PHE A 294     2520   2404   2963    -31     67     29       O  
ATOM   2250  CB  PHE A 294      18.915  21.143  29.630  1.00 22.29           C  
ANISOU 2250  CB  PHE A 294     2666   2586   3216    -27    134     42       C  
ATOM   2251  CG  PHE A 294      19.632  21.302  30.956  1.00 20.92           C  
ANISOU 2251  CG  PHE A 294     2451   2431   3066    -20    100     42       C  
ATOM   2252  CD1 PHE A 294      20.132  20.198  31.612  1.00 24.93           C  
ANISOU 2252  CD1 PHE A 294     2950   2944   3577      8     95     52       C  
ATOM   2253  CD2 PHE A 294      19.803  22.554  31.524  1.00 26.80           C  
ANISOU 2253  CD2 PHE A 294     3166   3188   3829    -39     75     31       C  
ATOM   2254  CE1 PHE A 294      20.789  20.331  32.837  1.00 33.11           C  
ANISOU 2254  CE1 PHE A 294     3946   4007   4627     20     61     52       C  
ATOM   2255  CE2 PHE A 294      20.473  22.699  32.738  1.00 27.02           C  
ANISOU 2255  CE2 PHE A 294     3153   3239   3874    -32     41     25       C  
ATOM   2256  CZ  PHE A 294      20.970  21.575  33.385  1.00 27.79           C  
ANISOU 2256  CZ  PHE A 294     3240   3350   3967     -1     32     36       C  
ATOM   2257  N   ALA A 295      15.839  21.766  30.177  1.00 20.56           N  
ANISOU 2257  N   ALA A 295     2516   2370   2925    -61     90     20       N  
ATOM   2258  CA  ALA A 295      14.905  22.453  31.056  1.00 18.55           C  
ANISOU 2258  CA  ALA A 295     2268   2124   2658    -76     57     12       C  
ATOM   2259  C   ALA A 295      13.840  21.512  31.598  1.00 21.34           C  
ANISOU 2259  C   ALA A 295     2650   2475   2982    -72     46      7       C  
ATOM   2260  O   ALA A 295      13.219  21.817  32.621  1.00 19.51           O  
ANISOU 2260  O   ALA A 295     2420   2252   2740    -77     17      3       O  
ATOM   2261  CB  ALA A 295      14.263  23.609  30.290  1.00 20.63           C  
ANISOU 2261  CB  ALA A 295     2541   2385   2912    -94     63      9       C  
ATOM   2262  N   LYS A 296      13.610  20.381  30.929  1.00 18.73           N  
ANISOU 2262  N   LYS A 296     2344   2132   2640    -63     70      6       N  
ATOM   2263  CA  LYS A 296      12.606  19.439  31.401  1.00 18.32           C  
ANISOU 2263  CA  LYS A 296     2319   2073   2569    -61     67      0       C  
ATOM   2264  C   LYS A 296      13.033  18.739  32.689  1.00 19.52           C  
ANISOU 2264  C   LYS A 296     2460   2225   2731    -41     55     13       C  
ATOM   2265  O   LYS A 296      12.181  18.137  33.356  1.00 21.02           O  
ANISOU 2265  O   LYS A 296     2670   2410   2908    -39     50     13       O  
ATOM   2266  CB  LYS A 296      12.264  18.432  30.287  1.00 19.01           C  
ANISOU 2266  CB  LYS A 296     2433   2144   2647    -60    100    -11       C  
ATOM   2267  CG  LYS A 296      11.680  19.162  29.060  1.00 18.82           C  
ANISOU 2267  CG  LYS A 296     2421   2128   2601    -76    107    -24       C  
ATOM   2268  CD  LYS A 296      11.167  18.202  27.943  1.00 18.90           C  
ANISOU 2268  CD  LYS A 296     2458   2130   2593    -78    134    -45       C  
ATOM   2269  CE  LYS A 296      11.176  18.873  26.542  1.00 20.11           C  
ANISOU 2269  CE  LYS A 296     2616   2298   2725    -81    148    -51       C  
ATOM   2270  NZ  LYS A 296      10.170  19.922  26.441  1.00 19.32           N  
ANISOU 2270  NZ  LYS A 296     2522   2218   2602    -94    126    -53       N  
ATOM   2271  N   THR A 297      14.302  18.872  33.097  1.00 19.66           N  
ANISOU 2271  N   THR A 297     2445   2254   2771    -24     49     26       N  
ATOM   2272  CA  THR A 297      14.684  18.409  34.435  1.00 19.19           C  
ANISOU 2272  CA  THR A 297     2371   2206   2714     -1     30     40       C  
ATOM   2273  C   THR A 297      13.932  19.157  35.530  1.00 18.63           C  
ANISOU 2273  C   THR A 297     2300   2154   2624    -11     -6     34       C  
ATOM   2274  O   THR A 297      13.897  18.697  36.680  1.00 22.39           O  
ANISOU 2274  O   THR A 297     2775   2642   3090      9    -22     46       O  
ATOM   2275  CB  THR A 297      16.200  18.549  34.669  1.00 22.45           C  
ANISOU 2275  CB  THR A 297     2742   2636   3154     18     25     51       C  
ATOM   2276  OG1 THR A 297      16.575  19.930  34.619  1.00 25.71           O  
ANISOU 2276  OG1 THR A 297     3125   3065   3579     -2      5     38       O  
ATOM   2277  CG2 THR A 297      16.989  17.771  33.597  1.00 22.48           C  
ANISOU 2277  CG2 THR A 297     2745   2620   3178     31     65     58       C  
ATOM   2278  N   SER A 298      13.273  20.259  35.171  1.00 19.30           N  
ANISOU 2278  N   SER A 298     2390   2242   2703    -39    -17     18       N  
ATOM   2279  CA  SER A 298      12.454  21.029  36.089  1.00 19.61           C  
ANISOU 2279  CA  SER A 298     2432   2294   2724    -51    -46      8       C  
ATOM   2280  C   SER A 298      11.365  20.198  36.753  1.00 21.86           C  
ANISOU 2280  C   SER A 298     2748   2574   2986    -44    -46     14       C  
ATOM   2281  O   SER A 298      10.898  20.558  37.850  1.00 20.43           O  
ANISOU 2281  O   SER A 298     2566   2408   2789    -42    -70     12       O  
ATOM   2282  CB  SER A 298      11.805  22.204  35.328  1.00 19.07           C  
ANISOU 2282  CB  SER A 298     2370   2221   2655    -80    -46     -6       C  
ATOM   2283  OG  SER A 298      11.061  21.713  34.219  1.00 25.57           O  
ANISOU 2283  OG  SER A 298     3222   3027   3466    -87    -21     -8       O  
ATOM   2284  N   ALA A 299      10.938  19.118  36.120  1.00 20.59           N  
ANISOU 2284  N   ALA A 299     2612   2389   2824    -41    -16     18       N  
ATOM   2285  CA  ALA A 299       9.884  18.297  36.690  1.00 23.65           C  
ANISOU 2285  CA  ALA A 299     3025   2764   3196    -38     -9     22       C  
ATOM   2286  C   ALA A 299      10.367  17.424  37.844  1.00 25.08           C  
ANISOU 2286  C   ALA A 299     3202   2949   3377     -4     -9     47       C  
ATOM   2287  O   ALA A 299       9.529  16.851  38.544  1.00 23.85           O  
ANISOU 2287  O   ALA A 299     3067   2785   3209      2     -2     55       O  
ATOM   2288  CB  ALA A 299       9.267  17.424  35.599  1.00 22.94           C  
ANISOU 2288  CB  ALA A 299     2960   2645   3110    -49     25     11       C  
ATOM   2289  N  AVAL A 300      11.685  17.318  38.063  0.43 20.34           N  
ANISOU 2289  N  AVAL A 300     2576   2363   2789     20    -14     61       N  
ATOM   2290  N  BVAL A 300      11.677  17.274  38.046  0.57 20.24           N  
ANISOU 2290  N  BVAL A 300     2564   2349   2777     20    -12     61       N  
ATOM   2291  CA AVAL A 300      12.216  16.347  39.018  0.43 25.29           C  
ANISOU 2291  CA AVAL A 300     3200   2995   3415     60     -9     90       C  
ATOM   2292  CA BVAL A 300      12.180  16.334  39.046  0.57 25.34           C  
ANISOU 2292  CA BVAL A 300     3207   3001   3421     60     -9     90       C  
ATOM   2293  C  AVAL A 300      13.080  16.970  40.118  0.43 23.13           C  
ANISOU 2293  C  AVAL A 300     2892   2765   3131     81    -47     97       C  
ATOM   2294  C  BVAL A 300      13.088  16.971  40.104  0.57 23.09           C  
ANISOU 2294  C  BVAL A 300     2887   2761   3127     81    -47     97       C  
ATOM   2295  O  AVAL A 300      13.165  16.429  41.225  0.43 26.02           O  
ANISOU 2295  O  AVAL A 300     3258   3148   3480    115    -54    120       O  
ATOM   2296  O  BVAL A 300      13.231  16.405  41.198  0.57 26.02           O  
ANISOU 2296  O  BVAL A 300     3258   3148   3482    116    -54    121       O  
ATOM   2297  CB AVAL A 300      13.015  15.255  38.275  0.43 24.61           C  
ANISOU 2297  CB AVAL A 300     3114   2884   3354     79     28    104       C  
ATOM   2298  CB BVAL A 300      12.903  15.143  38.375  0.57 24.66           C  
ANISOU 2298  CB BVAL A 300     3124   2888   3359     81     30    106       C  
ATOM   2299  CG1AVAL A 300      13.515  14.182  39.235  0.43 31.85           C  
ANISOU 2299  CG1AVAL A 300     4029   3803   4271    125     39    140       C  
ATOM   2300  CG1BVAL A 300      14.181  15.597  37.724  0.57 25.72           C  
ANISOU 2300  CG1BVAL A 300     3224   3035   3512     83     25    101       C  
ATOM   2301  CG2AVAL A 300      12.163  14.627  37.184  0.43 23.54           C  
ANISOU 2301  CG2AVAL A 300     3010   2708   3227     56     65     88       C  
ATOM   2302  CG2BVAL A 300      13.196  14.023  39.378  0.57 33.65           C  
ANISOU 2302  CG2BVAL A 300     4266   4025   4495    125     43    142       C  
ATOM   2303  N   TYR A 301      13.738  18.099  39.855  1.00 22.72           N  
ANISOU 2303  N   TYR A 301     2808   2734   3089     64    -72     76       N  
ATOM   2304  CA  TYR A 301      14.825  18.437  40.785  1.00 22.40           C  
ANISOU 2304  CA  TYR A 301     2729   2737   3047     89   -105     80       C  
ATOM   2305  C   TYR A 301      14.340  19.038  42.117  1.00 25.32           C  
ANISOU 2305  C   TYR A 301     3096   3142   3384     94   -142     72       C  
ATOM   2306  O   TYR A 301      15.060  18.939  43.105  1.00 25.16           O  
ANISOU 2306  O   TYR A 301     3050   3161   3350    125   -167     81       O  
ATOM   2307  CB  TYR A 301      15.882  19.347  40.118  1.00 23.44           C  
ANISOU 2307  CB  TYR A 301     2820   2878   3209     71   -115     60       C  
ATOM   2308  CG  TYR A 301      15.437  20.772  39.918  1.00 22.98           C  
ANISOU 2308  CG  TYR A 301     2756   2822   3154     31   -133     28       C  
ATOM   2309  CD1 TYR A 301      15.416  21.665  40.989  1.00 21.28           C  
ANISOU 2309  CD1 TYR A 301     2521   2641   2925     27   -172      8       C  
ATOM   2310  CD2 TYR A 301      15.070  21.236  38.669  1.00 25.33           C  
ANISOU 2310  CD2 TYR A 301     3067   3089   3467      0   -109     18       C  
ATOM   2311  CE1 TYR A 301      14.983  22.941  40.844  1.00 22.69           C  
ANISOU 2311  CE1 TYR A 301     2696   2816   3111     -8   -184    -20       C  
ATOM   2312  CE2 TYR A 301      14.651  22.556  38.502  1.00 25.11           C  
ANISOU 2312  CE2 TYR A 301     3034   3061   3444    -32   -121     -6       C  
ATOM   2313  CZ  TYR A 301      14.607  23.398  39.598  1.00 25.47           C  
ANISOU 2313  CZ  TYR A 301     3062   3134   3482    -37   -157    -25       C  
ATOM   2314  OH  TYR A 301      14.168  24.702  39.472  1.00 24.59           O  
ANISOU 2314  OH  TYR A 301     2948   3017   3380    -68   -165    -49       O  
ATOM   2315  N   ASN A 302      13.186  19.675  42.177  1.00 22.55           N  
ANISOU 2315  N   ASN A 302     2768   2781   3019     65   -147     55       N  
ATOM   2316  CA  ASN A 302      12.869  20.361  43.439  1.00 22.82           C  
ANISOU 2316  CA  ASN A 302     2796   2853   3024     70   -183     43       C  
ATOM   2317  C   ASN A 302      12.655  19.381  44.592  1.00 24.12           C  
ANISOU 2317  C   ASN A 302     2975   3034   3154    113   -183     74       C  
ATOM   2318  O   ASN A 302      13.135  19.643  45.700  1.00 25.17           O  
ANISOU 2318  O   ASN A 302     3087   3214   3262    138   -216     72       O  
ATOM   2319  CB  ASN A 302      11.656  21.293  43.298  1.00 23.40           C  
ANISOU 2319  CB  ASN A 302     2890   2911   3089     33   -186     19       C  
ATOM   2320  CG  ASN A 302      11.995  22.596  42.619  1.00 25.38           C  
ANISOU 2320  CG  ASN A 302     3118   3160   3367     -2   -198    -13       C  
ATOM   2321  OD1 ASN A 302      12.746  23.408  43.148  1.00 24.07           O  
ANISOU 2321  OD1 ASN A 302     2916   3023   3207     -4   -227    -34       O  
ATOM   2322  ND2 ASN A 302      11.434  22.809  41.425  1.00 22.68           N  
ANISOU 2322  ND2 ASN A 302     2792   2782   3041    -29   -173    -16       N  
ATOM   2323  N   PRO A 303      11.941  18.264  44.396  1.00 22.34           N  
ANISOU 2323  N   PRO A 303     2786   2774   2927    124   -145    102       N  
ATOM   2324  CA  PRO A 303      11.853  17.267  45.477  1.00 20.75           C  
ANISOU 2324  CA  PRO A 303     2600   2587   2699    170   -136    140       C  
ATOM   2325  C   PRO A 303      13.182  16.681  45.905  1.00 26.61           C  
ANISOU 2325  C   PRO A 303     3313   3359   3440    217   -145    165       C  
ATOM   2326  O   PRO A 303      13.298  16.234  47.047  1.00 28.53           O  
ANISOU 2326  O   PRO A 303     3557   3635   3650    262   -154    193       O  
ATOM   2327  CB  PRO A 303      10.949  16.181  44.876  1.00 30.67           C  
ANISOU 2327  CB  PRO A 303     3895   3787   3970    165    -85    160       C  
ATOM   2328  CG  PRO A 303      10.126  16.897  43.891  1.00 27.18           C  
ANISOU 2328  CG  PRO A 303     3464   3320   3545    113    -81    125       C  
ATOM   2329  CD  PRO A 303      11.029  17.930  43.277  1.00 20.31           C  
ANISOU 2329  CD  PRO A 303     2560   2467   2690     93   -108     98       C  
ATOM   2330  N   VAL A 304      14.160  16.586  45.000  1.00 26.28           N  
ANISOU 2330  N   VAL A 304     3246   3307   3432    213   -138    161       N  
ATOM   2331  CA  VAL A 304      15.486  16.094  45.383  1.00 20.77           C  
ANISOU 2331  CA  VAL A 304     2515   2642   2736    259   -148    184       C  
ATOM   2332  C   VAL A 304      16.159  17.071  46.346  1.00 21.05           C  
ANISOU 2332  C   VAL A 304     2507   2744   2747    269   -205    161       C  
ATOM   2333  O   VAL A 304      16.674  16.678  47.403  1.00 24.60           O  
ANISOU 2333  O   VAL A 304     2941   3241   3166    318   -225    184       O  
ATOM   2334  CB  VAL A 304      16.347  15.887  44.118  1.00 29.75           C  
ANISOU 2334  CB  VAL A 304     3634   3752   3919    247   -126    179       C  
ATOM   2335  CG1 VAL A 304      17.765  15.415  44.525  1.00 27.26           C  
ANISOU 2335  CG1 VAL A 304     3276   3473   3608    296   -138    202       C  
ATOM   2336  CG2 VAL A 304      15.682  14.914  43.170  1.00 26.98           C  
ANISOU 2336  CG2 VAL A 304     3324   3337   3590    237    -71    194       C  
ATOM   2337  N   ILE A 305      16.157  18.365  45.992  1.00 22.88           N  
ANISOU 2337  N   ILE A 305     2719   2982   2992    222   -231    114       N  
ATOM   2338  CA  ILE A 305      16.639  19.395  46.919  1.00 21.26           C  
ANISOU 2338  CA  ILE A 305     2476   2837   2767    223   -284     81       C  
ATOM   2339  C   ILE A 305      15.929  19.277  48.263  1.00 21.67           C  
ANISOU 2339  C   ILE A 305     2547   2923   2762    251   -302     92       C  
ATOM   2340  O   ILE A 305      16.554  19.357  49.320  1.00 22.29           O  
ANISOU 2340  O   ILE A 305     2598   3064   2809    287   -339     90       O  
ATOM   2341  CB  ILE A 305      16.414  20.803  46.331  1.00 21.39           C  
ANISOU 2341  CB  ILE A 305     2480   2839   2809    164   -297     30       C  
ATOM   2342  CG1 ILE A 305      17.207  21.012  45.033  1.00 25.65           C  
ANISOU 2342  CG1 ILE A 305     2995   3349   3402    138   -278     21       C  
ATOM   2343  CG2 ILE A 305      16.779  21.872  47.403  1.00 25.32           C  
ANISOU 2343  CG2 ILE A 305     2940   3395   3285    161   -350    -11       C  
ATOM   2344  CD1 ILE A 305      16.859  22.370  44.342  1.00 25.77           C  
ANISOU 2344  CD1 ILE A 305     3006   3341   3445     82   -279    -20       C  
ATOM   2345  N   TYR A 306      14.613  19.101  48.225  1.00 22.89           N  
ANISOU 2345  N   TYR A 306     2751   3041   2905    236   -276    101       N  
ATOM   2346  CA  TYR A 306      13.804  19.008  49.443  1.00 23.96           C  
ANISOU 2346  CA  TYR A 306     2912   3204   2989    260   -285    113       C  
ATOM   2347  C   TYR A 306      14.319  17.914  50.363  1.00 26.64           C  
ANISOU 2347  C   TYR A 306     3249   3578   3294    329   -283    162       C  
ATOM   2348  O   TYR A 306      14.548  18.140  51.560  1.00 26.58           O  
ANISOU 2348  O   TYR A 306     3227   3632   3238    363   -319    160       O  
ATOM   2349  CB  TYR A 306      12.357  18.738  49.028  1.00 23.19           C  
ANISOU 2349  CB  TYR A 306     2865   3051   2896    234   -245    123       C  
ATOM   2350  CG  TYR A 306      11.243  18.971  50.057  1.00 21.86           C  
ANISOU 2350  CG  TYR A 306     2725   2897   2684    240   -250    123       C  
ATOM   2351  CD1 TYR A 306      11.427  19.737  51.208  1.00 23.41           C  
ANISOU 2351  CD1 TYR A 306     2902   3153   2837    255   -294    101       C  
ATOM   2352  CD2 TYR A 306       9.967  18.453  49.806  1.00 25.16           C  
ANISOU 2352  CD2 TYR A 306     3186   3266   3107    227   -208    142       C  
ATOM   2353  CE1 TYR A 306      10.338  19.963  52.105  1.00 23.18           C  
ANISOU 2353  CE1 TYR A 306     2903   3136   2769    260   -293    100       C  
ATOM   2354  CE2 TYR A 306       8.915  18.671  50.654  1.00 25.22           C  
ANISOU 2354  CE2 TYR A 306     3219   3283   3081    229   -207    143       C  
ATOM   2355  CZ  TYR A 306       9.092  19.429  51.789  1.00 28.26           C  
ANISOU 2355  CZ  TYR A 306     3589   3726   3421    246   -248    123       C  
ATOM   2356  OH  TYR A 306       7.999  19.610  52.590  1.00 28.96           O  
ANISOU 2356  OH  TYR A 306     3706   3822   3477    250   -241    125       O  
ATOM   2357  N   ILE A 307      14.569  16.732  49.805  1.00 25.40           N  
ANISOU 2357  N   ILE A 307     3106   3385   3162    352   -242    204       N  
ATOM   2358  CA  ILE A 307      15.011  15.607  50.618  1.00 22.37           C  
ANISOU 2358  CA  ILE A 307     2724   3026   2749    421   -231    260       C  
ATOM   2359  C   ILE A 307      16.391  15.885  51.208  1.00 26.17           C  
ANISOU 2359  C   ILE A 307     3151   3581   3213    458   -280    253       C  
ATOM   2360  O   ILE A 307      16.670  15.554  52.366  1.00 29.57           O  
ANISOU 2360  O   ILE A 307     3574   4069   3594    516   -300    280       O  
ATOM   2361  CB  ILE A 307      15.018  14.334  49.759  1.00 27.81           C  
ANISOU 2361  CB  ILE A 307     3438   3651   3479    432   -171    301       C  
ATOM   2362  CG1 ILE A 307      13.597  13.914  49.383  1.00 37.46           C  
ANISOU 2362  CG1 ILE A 307     4712   4807   4712    403   -123    309       C  
ATOM   2363  CG2 ILE A 307      15.740  13.216  50.453  1.00 33.66           C  
ANISOU 2363  CG2 ILE A 307     4173   4416   4202    507   -158    360       C  
ATOM   2364  CD1 ILE A 307      13.596  12.851  48.294  1.00 35.64           C  
ANISOU 2364  CD1 ILE A 307     4500   4508   4531    397    -66    330       C  
ATOM   2365  N   MET A 308      17.280  16.478  50.409  1.00 28.33           N  
ANISOU 2365  N   MET A 308     3383   3856   3527    428   -298    217       N  
ATOM   2366  CA  MET A 308      18.645  16.710  50.854  1.00 27.23           C  
ANISOU 2366  CA  MET A 308     3182   3782   3380    459   -343    207       C  
ATOM   2367  C   MET A 308      18.725  17.815  51.902  1.00 29.62           C  
ANISOU 2367  C   MET A 308     3456   4157   3640    455   -404    160       C  
ATOM   2368  O   MET A 308      19.662  17.838  52.706  1.00 34.01           O  
ANISOU 2368  O   MET A 308     3968   4787   4168    498   -446    158       O  
ATOM   2369  CB  MET A 308      19.514  17.062  49.645  1.00 27.22           C  
ANISOU 2369  CB  MET A 308     3146   3756   3442    422   -339    180       C  
ATOM   2370  CG  MET A 308      19.670  15.914  48.645  1.00 40.36           C  
ANISOU 2370  CG  MET A 308     4830   5359   5145    434   -282    223       C  
ATOM   2371  SD  MET A 308      20.660  16.432  47.225  1.00 65.77           S  
ANISOU 2371  SD  MET A 308     8008   8550   8432    390   -275    190       S  
ATOM   2372  CE  MET A 308      22.006  17.264  48.063  1.00 55.18           C  
ANISOU 2372  CE  MET A 308     6586   7299   7081    408   -343    156       C  
ATOM   2373  N   MET A 309      17.785  18.755  51.902  1.00 26.20           N  
ANISOU 2373  N   MET A 309     3045   3708   3204    405   -411    120       N  
ATOM   2374  CA  MET A 309      17.985  19.979  52.662  1.00 31.82           C  
ANISOU 2374  CA  MET A 309     3722   4479   3890    388   -467     61       C  
ATOM   2375  C   MET A 309      16.899  20.259  53.683  1.00 36.59           C  
ANISOU 2375  C   MET A 309     4362   5104   4437    396   -476     56       C  
ATOM   2376  O   MET A 309      16.913  21.336  54.294  1.00 31.86           O  
ANISOU 2376  O   MET A 309     3740   4548   3818    376   -518      0       O  
ATOM   2377  CB  MET A 309      18.115  21.173  51.715  1.00 26.77           C  
ANISOU 2377  CB  MET A 309     3059   3806   3308    317   -472      2       C  
ATOM   2378  CG  MET A 309      19.300  21.046  50.771  1.00 29.33           C  
ANISOU 2378  CG  MET A 309     3339   4116   3687    309   -466      1       C  
ATOM   2379  SD  MET A 309      19.580  22.610  49.917  1.00 27.45           S  
ANISOU 2379  SD  MET A 309     3066   3854   3511    231   -478    -70       S  
ATOM   2380  CE  MET A 309      20.297  23.569  51.262  1.00 24.36           C  
ANISOU 2380  CE  MET A 309     2614   3553   3087    240   -549   -131       C  
ATOM   2381  N   ASN A 310      15.950  19.349  53.888  1.00 28.74           N  
ANISOU 2381  N   ASN A 310     3422   4079   3419    421   -435    108       N  
ATOM   2382  CA  ASN A 310      14.934  19.559  54.925  1.00 26.49           C  
ANISOU 2382  CA  ASN A 310     3171   3816   3077    434   -440    108       C  
ATOM   2383  C   ASN A 310      14.870  18.298  55.784  1.00 31.62           C  
ANISOU 2383  C   ASN A 310     3845   4491   3677    510   -419    179       C  
ATOM   2384  O   ASN A 310      14.339  17.265  55.364  1.00 24.25           O  
ANISOU 2384  O   ASN A 310     2951   3500   2762    522   -364    232       O  
ATOM   2385  CB  ASN A 310      13.568  19.924  54.330  1.00 25.26           C  
ANISOU 2385  CB  ASN A 310     3060   3592   2946    380   -404     97       C  
ATOM   2386  CG  ASN A 310      12.574  20.410  55.409  1.00 37.85           C  
ANISOU 2386  CG  ASN A 310     4681   5214   4485    386   -415     84       C  
ATOM   2387  OD1 ASN A 310      11.835  19.614  56.000  1.00 30.99           O  
ANISOU 2387  OD1 ASN A 310     3853   4341   3582    422   -385    131       O  
ATOM   2388  ND2 ASN A 310      12.580  21.710  55.680  1.00 33.01           N  
ANISOU 2388  ND2 ASN A 310     4046   4629   3867    351   -455     19       N  
ATOM   2389  N   LYS A 311      15.432  18.394  56.987  1.00 26.44           N  
ANISOU 2389  N   LYS A 311     3164   3923   2959    562   -463    177       N  
ATOM   2390  CA  LYS A 311      15.554  17.229  57.853  1.00 30.79           C  
ANISOU 2390  CA  LYS A 311     3733   4509   3458    644   -447    248       C  
ATOM   2391  C   LYS A 311      14.184  16.666  58.196  1.00 27.43           C  
ANISOU 2391  C   LYS A 311     3372   4040   3011    654   -394    293       C  
ATOM   2392  O   LYS A 311      13.975  15.449  58.188  1.00 34.16           O  
ANISOU 2392  O   LYS A 311     4255   4858   3866    696   -342    363       O  
ATOM   2393  CB  LYS A 311      16.314  17.635  59.119  1.00 33.86           C  
ANISOU 2393  CB  LYS A 311     4081   5009   3774    695   -511    228       C  
ATOM   2394  CG  LYS A 311      16.602  16.536  60.119  1.00 42.97           C  
ANISOU 2394  CG  LYS A 311     5245   6218   4864    790   -503    302       C  
ATOM   2395  CD  LYS A 311      17.295  17.138  61.335  1.00 52.69           C  
ANISOU 2395  CD  LYS A 311     6432   7568   6018    833   -576    267       C  
ATOM   2396  CE  LYS A 311      17.621  16.094  62.395  1.00 60.69           C  
ANISOU 2396  CE  LYS A 311     7454   8649   6958    937   -572    343       C  
ATOM   2397  NZ  LYS A 311      18.244  16.734  63.598  1.00 64.94           N  
ANISOU 2397  NZ  LYS A 311     7949   9313   7413    979   -648    301       N  
ATOM   2398  N   GLN A 312      13.243  17.540  58.512  1.00 26.28           N  
ANISOU 2398  N   GLN A 312     3246   3893   2847    616   -403    252       N  
ATOM   2399  CA  GLN A 312      11.936  17.075  58.948  1.00 31.31           C  
ANISOU 2399  CA  GLN A 312     3940   4497   3461    627   -356    290       C  
ATOM   2400  C   GLN A 312      11.236  16.311  57.832  1.00 35.09           C  
ANISOU 2400  C   GLN A 312     4453   4874   4006    594   -289    323       C  
ATOM   2401  O   GLN A 312      10.678  15.234  58.057  1.00 31.24           O  
ANISOU 2401  O   GLN A 312     4003   4353   3513    629   -235    386       O  
ATOM   2402  CB  GLN A 312      11.106  18.265  59.398  1.00 29.54           C  
ANISOU 2402  CB  GLN A 312     3724   4288   3210    587   -380    233       C  
ATOM   2403  CG  GLN A 312       9.720  17.907  59.899  1.00 40.63           C  
ANISOU 2403  CG  GLN A 312     5184   5663   4591    596   -332    267       C  
ATOM   2404  CD  GLN A 312       8.948  19.132  60.340  1.00 46.50           C  
ANISOU 2404  CD  GLN A 312     5933   6425   5311    558   -357    208       C  
ATOM   2405  OE1 GLN A 312       8.730  20.058  59.557  1.00 51.99           O  
ANISOU 2405  OE1 GLN A 312     6616   7085   6053    492   -369    152       O  
ATOM   2406  NE2 GLN A 312       8.550  19.157  61.610  1.00 54.21           N  
ANISOU 2406  NE2 GLN A 312     6928   7457   6214    604   -362    220       N  
ATOM   2407  N   PHE A 313      11.271  16.846  56.607  1.00 25.21           N  
ANISOU 2407  N   PHE A 313     3188   3572   2818    527   -291    280       N  
ATOM   2408  CA  PHE A 313      10.622  16.141  55.512  1.00 24.81           C  
ANISOU 2408  CA  PHE A 313     3167   3432   2827    495   -232    303       C  
ATOM   2409  C   PHE A 313      11.323  14.818  55.226  1.00 29.14           C  
ANISOU 2409  C   PHE A 313     3717   3960   3397    540   -197    362       C  
ATOM   2410  O   PHE A 313      10.663  13.791  55.012  1.00 29.78           O  
ANISOU 2410  O   PHE A 313     3835   3983   3499    550   -136    407       O  
ATOM   2411  CB  PHE A 313      10.570  17.009  54.258  1.00 24.84           C  
ANISOU 2411  CB  PHE A 313     3156   3395   2888    421   -243    246       C  
ATOM   2412  CG  PHE A 313      10.050  16.264  53.064  1.00 29.94           C  
ANISOU 2412  CG  PHE A 313     3826   3958   3590    391   -188    265       C  
ATOM   2413  CD1 PHE A 313       8.697  15.976  52.953  1.00 37.85           C  
ANISOU 2413  CD1 PHE A 313     4869   4911   4602    369   -146    276       C  
ATOM   2414  CD2 PHE A 313      10.908  15.814  52.077  1.00 30.64           C  
ANISOU 2414  CD2 PHE A 313     3897   4021   3724    386   -178    270       C  
ATOM   2415  CE1 PHE A 313       8.206  15.253  51.878  1.00 26.88           C  
ANISOU 2415  CE1 PHE A 313     3500   3450   3264    341    -97    287       C  
ATOM   2416  CE2 PHE A 313      10.420  15.080  50.988  1.00 31.34           C  
ANISOU 2416  CE2 PHE A 313     4010   4037   3862    360   -127    283       C  
ATOM   2417  CZ  PHE A 313       9.061  14.816  50.891  1.00 32.23           C  
ANISOU 2417  CZ  PHE A 313     4161   4104   3982    336    -89    288       C  
ATOM   2418  N   ARG A 314      12.659  14.807  55.277  1.00 31.19           N  
ANISOU 2418  N   ARG A 314     3934   4266   3651    570   -232    361       N  
ATOM   2419  CA  ARG A 314      13.394  13.576  55.025  1.00 32.30           C  
ANISOU 2419  CA  ARG A 314     4072   4389   3812    618   -198    418       C  
ATOM   2420  C   ARG A 314      13.026  12.502  56.039  1.00 34.57           C  
ANISOU 2420  C   ARG A 314     4393   4685   4058    689   -160    491       C  
ATOM   2421  O   ARG A 314      12.847  11.331  55.675  1.00 33.87           O  
ANISOU 2421  O   ARG A 314     4331   4536   4002    709    -98    543       O  
ATOM   2422  CB  ARG A 314      14.903  13.847  55.070  1.00 32.51           C  
ANISOU 2422  CB  ARG A 314     4040   4478   3834    644   -249    403       C  
ATOM   2423  CG  ARG A 314      15.752  12.638  54.732  1.00 39.86           C  
ANISOU 2423  CG  ARG A 314     4964   5390   4791    693   -216    459       C  
ATOM   2424  CD  ARG A 314      17.188  13.065  54.446  1.00 44.39           C  
ANISOU 2424  CD  ARG A 314     5475   6013   5379    698   -264    431       C  
ATOM   2425  NE  ARG A 314      17.824  13.661  55.612  1.00 38.64           N  
ANISOU 2425  NE  ARG A 314     4707   5387   4588    738   -329    415       N  
ATOM   2426  CZ  ARG A 314      18.162  14.940  55.738  1.00 39.79           C  
ANISOU 2426  CZ  ARG A 314     4812   5581   4724    699   -390    344       C  
ATOM   2427  NH1 ARG A 314      17.930  15.826  54.778  1.00 35.78           N  
ANISOU 2427  NH1 ARG A 314     4299   5030   4268    621   -393    286       N  
ATOM   2428  NH2 ARG A 314      18.755  15.341  56.856  1.00 37.45           N  
ANISOU 2428  NH2 ARG A 314     4480   5381   4367    742   -447    330       N  
ATOM   2429  N   ASN A 315      12.940  12.878  57.322  1.00 32.56           N  
ANISOU 2429  N   ASN A 315     4137   4504   3730    730   -193    495       N  
ATOM   2430  CA  ASN A 315      12.579  11.913  58.351  1.00 35.63           C  
ANISOU 2430  CA  ASN A 315     4559   4905   4072    802   -154    569       C  
ATOM   2431  C   ASN A 315      11.165  11.389  58.147  1.00 34.19           C  
ANISOU 2431  C   ASN A 315     4431   4641   3917    776    -85    594       C  
ATOM   2432  O   ASN A 315      10.932  10.183  58.289  1.00 37.52           O  
ANISOU 2432  O   ASN A 315     4884   5021   4351    819    -21    662       O  
ATOM   2433  CB  ASN A 315      12.737  12.540  59.737  1.00 38.22           C  
ANISOU 2433  CB  ASN A 315     4874   5335   4311    848   -208    561       C  
ATOM   2434  CG  ASN A 315      14.182  12.792  60.086  1.00 45.03           C  
ANISOU 2434  CG  ASN A 315     5681   6286   5144    890   -271    548       C  
ATOM   2435  OD1 ASN A 315      15.080  12.242  59.449  1.00 49.33           O  
ANISOU 2435  OD1 ASN A 315     6200   6814   5728    903   -264    567       O  
ATOM   2436  ND2 ASN A 315      14.423  13.608  61.105  1.00 51.90           N  
ANISOU 2436  ND2 ASN A 315     6528   7251   5942    912   -333    514       N  
ATOM   2437  N   CYS A 316      10.210  12.270  57.821  1.00 28.30           N  
ANISOU 2437  N   CYS A 316     3698   3871   3186    708    -93    539       N  
ATOM   2438  CA  CYS A 316       8.855  11.796  57.552  1.00 32.00           C  
ANISOU 2438  CA  CYS A 316     4212   4262   3686    678    -28    556       C  
ATOM   2439  C   CYS A 316       8.839  10.865  56.357  1.00 36.00           C  
ANISOU 2439  C   CYS A 316     4729   4681   4270    653     26    573       C  
ATOM   2440  O   CYS A 316       8.129   9.856  56.355  1.00 38.08           O  
ANISOU 2440  O   CYS A 316     5027   4884   4558    665     95    619       O  
ATOM   2441  CB  CYS A 316       7.894  12.958  57.287  1.00 33.72           C  
ANISOU 2441  CB  CYS A 316     4434   4469   3909    607    -50    491       C  
ATOM   2442  SG  CYS A 316       7.641  14.050  58.653  1.00 46.05           S  
ANISOU 2442  SG  CYS A 316     5992   6119   5387    627   -102    464       S  
ATOM   2443  N   MET A 317       9.603  11.198  55.321  1.00 31.34           N  
ANISOU 2443  N   MET A 317     4108   4082   3720    617      0    534       N  
ATOM   2444  CA  MET A 317       9.602  10.345  54.145  1.00 35.20           C  
ANISOU 2444  CA  MET A 317     4606   4491   4279    593     50    543       C  
ATOM   2445  C   MET A 317      10.141   8.965  54.474  1.00 39.20           C  
ANISOU 2445  C   MET A 317     5123   4979   4791    662    100    617       C  
ATOM   2446  O   MET A 317       9.557   7.954  54.073  1.00 35.52           O  
ANISOU 2446  O   MET A 317     4688   4438   4371    658    169    647       O  
ATOM   2447  CB  MET A 317      10.413  10.980  53.027  1.00 28.60           C  
ANISOU 2447  CB  MET A 317     3734   3655   3478    549     12    491       C  
ATOM   2448  CG  MET A 317      10.279  10.189  51.744  1.00 50.18           C  
ANISOU 2448  CG  MET A 317     6480   6306   6280    517     64    491       C  
ATOM   2449  SD  MET A 317      11.538  10.732  50.621  1.00 65.79           S  
ANISOU 2449  SD  MET A 317     8413   8295   8290    490     26    449       S  
ATOM   2450  CE  MET A 317      12.941  10.652  51.732  1.00 55.11           C  
ANISOU 2450  CE  MET A 317     7024   7027   6889    570    -15    486       C  
ATOM   2451  N   VAL A 318      11.235   8.903  55.240  1.00 33.34           N  
ANISOU 2451  N   VAL A 318     4356   4308   4005    728     66    647       N  
ATOM   2452  CA  VAL A 318      11.770   7.614  55.658  1.00 38.75           C  
ANISOU 2452  CA  VAL A 318     5051   4982   4690    804    113    725       C  
ATOM   2453  C   VAL A 318      10.758   6.876  56.524  1.00 45.92           C  
ANISOU 2453  C   VAL A 318     6005   5864   5579    840    173    783       C  
ATOM   2454  O   VAL A 318      10.603   5.653  56.414  1.00 42.14           O  
ANISOU 2454  O   VAL A 318     5552   5321   5137    869    247    840       O  
ATOM   2455  CB  VAL A 318      13.112   7.802  56.386  1.00 37.68           C  
ANISOU 2455  CB  VAL A 318     4874   4941   4502    871     57    744       C  
ATOM   2456  CG1 VAL A 318      13.596   6.486  56.931  1.00 40.70           C  
ANISOU 2456  CG1 VAL A 318     5269   5318   4878    959    107    832       C  
ATOM   2457  CG2 VAL A 318      14.135   8.379  55.436  1.00 46.44           C  
ANISOU 2457  CG2 VAL A 318     5936   6063   5645    835     11    691       C  
ATOM   2458  N   THR A 319      10.044   7.607  57.386  1.00 36.51           N  
ANISOU 2458  N   THR A 319     4824   4717   4332    837    148    770       N  
ATOM   2459  CA  THR A 319       9.055   6.983  58.263  1.00 43.60           C  
ANISOU 2459  CA  THR A 319     5765   5593   5207    871    206    825       C  
ATOM   2460  C   THR A 319       7.931   6.342  57.459  1.00 50.10           C  
ANISOU 2460  C   THR A 319     6621   6307   6106    816    281    823       C  
ATOM   2461  O   THR A 319       7.538   5.196  57.716  1.00 55.61           O  
ANISOU 2461  O   THR A 319     7350   6950   6827    852    358    886       O  
ATOM   2462  CB  THR A 319       8.496   8.022  59.242  1.00 48.24           C  
ANISOU 2462  CB  THR A 319     6355   6250   5723    870    160    799       C  
ATOM   2463  OG1 THR A 319       9.474   8.293  60.249  1.00 50.08           O  
ANISOU 2463  OG1 THR A 319     6564   6585   5878    941    106    818       O  
ATOM   2464  CG2 THR A 319       7.212   7.535  59.910  1.00 56.16           C  
ANISOU 2464  CG2 THR A 319     7404   7215   6717    882    225    841       C  
ATOM   2465  N   THR A 320       7.406   7.068  56.474  1.00 40.64           N  
ANISOU 2465  N   THR A 320     5416   5078   4948    731    260    750       N  
ATOM   2466  CA  THR A 320       6.343   6.535  55.628  1.00 51.74           C  
ANISOU 2466  CA  THR A 320     6847   6388   6424    674    323    736       C  
ATOM   2467  C   THR A 320       6.825   5.365  54.783  1.00 56.38           C  
ANISOU 2467  C   THR A 320     7438   6906   7079    680    378    761       C  
ATOM   2468  O   THR A 320       6.131   4.350  54.654  1.00 62.57           O  
ANISOU 2468  O   THR A 320     8250   7613   7911    678    456    791       O  
ATOM   2469  CB  THR A 320       5.815   7.637  54.727  1.00 44.44           C  
ANISOU 2469  CB  THR A 320     5907   5458   5519    588    280    653       C  
ATOM   2470  OG1 THR A 320       5.271   8.681  55.535  1.00 50.38           O  
ANISOU 2470  OG1 THR A 320     6660   6268   6216    582    238    631       O  
ATOM   2471  CG2 THR A 320       4.763   7.099  53.759  1.00 48.28           C  
ANISOU 2471  CG2 THR A 320     6413   5853   6078    528    338    631       C  
ATOM   2472  N   LEU A 321       8.005   5.501  54.177  1.00 46.93           N  
ANISOU 2472  N   LEU A 321     6210   5731   5890    685    341    744       N  
ATOM   2473  CA  LEU A 321       8.496   4.502  53.237  1.00 54.68           C  
ANISOU 2473  CA  LEU A 321     7193   6646   6937    684    389    756       C  
ATOM   2474  C   LEU A 321       8.969   3.238  53.939  1.00 53.25           C  
ANISOU 2474  C   LEU A 321     7028   6448   6758    768    448    843       C  
ATOM   2475  O   LEU A 321       9.117   2.199  53.289  1.00 56.32           O  
ANISOU 2475  O   LEU A 321     7427   6762   7208    770    510    862       O  
ATOM   2476  CB  LEU A 321       9.634   5.099  52.405  1.00 48.42           C  
ANISOU 2476  CB  LEU A 321     6361   5886   6150    666    331    712       C  
ATOM   2477  CG  LEU A 321       9.647   4.839  50.903  1.00 51.69           C  
ANISOU 2477  CG  LEU A 321     6773   6234   6635    607    354    667       C  
ATOM   2478  CD1 LEU A 321       8.348   5.322  50.303  1.00 56.76           C  
ANISOU 2478  CD1 LEU A 321     7430   6838   7299    530    359    611       C  
ATOM   2479  CD2 LEU A 321      10.824   5.523  50.237  1.00 61.03           C  
ANISOU 2479  CD2 LEU A 321     7915   7459   7815    597    296    631       C  
ATOM   2480  N   CYS A 322       9.200   3.306  55.244  1.00 53.01           N  
ANISOU 2480  N   CYS A 322     7000   6483   6659    838    433    896       N  
ATOM   2481  CA  CYS A 322       9.758   2.194  56.004  1.00 62.39           C  
ANISOU 2481  CA  CYS A 322     8201   7669   7837    930    483    986       C  
ATOM   2482  C   CYS A 322       8.855   1.830  57.172  1.00 58.62           C  
ANISOU 2482  C   CYS A 322     7759   7190   7324    971    529   1044       C  
ATOM   2483  O   CYS A 322       9.316   1.700  58.303  1.00 77.71           O  
ANISOU 2483  O   CYS A 322    10178   9673   9676   1054    520   1106       O  
ATOM   2484  CB  CYS A 322      11.164   2.549  56.503  1.00 52.26           C  
ANISOU 2484  CB  CYS A 322     6879   6482   6496    994    416   1005       C  
ATOM   2485  SG  CYS A 322      12.233   3.223  55.190  1.00 71.68           S  
ANISOU 2485  SG  CYS A 322     9289   8955   8990    941    353    929       S  
TER    2486      CYS A 322                                                      
ATOM   2487  N   MET B   1     -14.529  22.545  70.550  1.00 30.26           N  
ANISOU 2487  N   MET B   1     4377   4115   3006    537    407    330       N  
ATOM   2488  CA  MET B   1     -14.650  23.371  69.336  1.00 29.32           C  
ANISOU 2488  CA  MET B   1     4224   3957   2959    466    365    268       C  
ATOM   2489  C   MET B   1     -13.790  24.625  69.465  1.00 30.13           C  
ANISOU 2489  C   MET B   1     4316   4115   3019    462    286    196       C  
ATOM   2490  O   MET B   1     -13.596  25.139  70.550  1.00 35.05           O  
ANISOU 2490  O   MET B   1     4956   4800   3563    502    273    178       O  
ATOM   2491  CB  MET B   1     -16.107  23.766  69.089  1.00 37.76           C  
ANISOU 2491  CB  MET B   1     5285   4979   4082    429    408    256       C  
ATOM   2492  N   ASN B   2     -13.275  25.121  68.348  1.00 32.08           N  
ANISOU 2492  N   ASN B   2     4533   4338   3318    412    236    153       N  
ATOM   2493  CA  ASN B   2     -12.451  26.308  68.379  1.00 30.67           C  
ANISOU 2493  CA  ASN B   2     4340   4202   3112    402    167     83       C  
ATOM   2494  C   ASN B   2     -13.206  27.573  67.998  1.00 38.52           C  
ANISOU 2494  C   ASN B   2     5320   5172   4145    357    159     24       C  
ATOM   2495  O   ASN B   2     -12.610  28.656  67.993  1.00 40.60           O  
ANISOU 2495  O   ASN B   2     5570   5461   4395    344    107    -38       O  
ATOM   2496  CB  ASN B   2     -11.246  26.102  67.472  1.00 29.51           C  
ANISOU 2496  CB  ASN B   2     4170   4050   2993    382    118     74       C  
ATOM   2497  CG  ASN B   2     -10.260  25.119  68.072  1.00 35.57           C  
ANISOU 2497  CG  ASN B   2     4950   4862   3705    437    112    119       C  
ATOM   2498  OD1 ASN B   2      -9.522  25.469  68.997  1.00 34.31           O  
ANISOU 2498  OD1 ASN B   2     4795   4772   3468    477     77     99       O  
ATOM   2499  ND2 ASN B   2     -10.253  23.882  67.567  1.00 30.96           N  
ANISOU 2499  ND2 ASN B   2     4370   4238   3158    441    148    180       N  
ATOM   2500  N   GLY B   3     -14.489  27.462  67.671  1.00 30.57           N  
ANISOU 2500  N   GLY B   3     4312   4114   3188    335    209     42       N  
ATOM   2501  CA  GLY B   3     -15.303  28.623  67.377  1.00 27.37           C  
ANISOU 2501  CA  GLY B   3     3894   3687   2817    300    208     -6       C  
ATOM   2502  C   GLY B   3     -16.519  28.645  68.273  1.00 30.55           C  
ANISOU 2502  C   GLY B   3     4317   4092   3198    323    266     12       C  
ATOM   2503  O   GLY B   3     -16.573  27.907  69.254  1.00 31.53           O  
ANISOU 2503  O   GLY B   3     4468   4245   3267    370    300     55       O  
ATOM   2504  N   THR B   4     -17.513  29.458  67.936  1.00 23.30           N  
ANISOU 2504  N   THR B   4     3386   3142   2324    293    281    -16       N  
ATOM   2505  CA  THR B   4     -18.687  29.643  68.779  1.00 25.03           C  
ANISOU 2505  CA  THR B   4     3620   3364   2526    313    335     -7       C  
ATOM   2506  C   THR B   4     -19.942  29.365  67.972  1.00 30.39           C  
ANISOU 2506  C   THR B   4     4279   3983   3287    278    379     16       C  
ATOM   2507  O   THR B   4     -20.237  30.081  67.013  1.00 27.80           O  
ANISOU 2507  O   THR B   4     3922   3623   3016    237    358    -17       O  
ATOM   2508  CB  THR B   4     -18.708  31.067  69.340  1.00 28.95           C  
ANISOU 2508  CB  THR B   4     4120   3888   2989    316    311    -72       C  
ATOM   2509  OG1 THR B   4     -17.452  31.304  69.988  1.00 29.68           O  
ANISOU 2509  OG1 THR B   4     4225   4040   3010    344    262   -102       O  
ATOM   2510  CG2 THR B   4     -19.871  31.241  70.361  1.00 27.21           C  
ANISOU 2510  CG2 THR B   4     3921   3678   2740    345    370    -62       C  
ATOM   2511  N   GLU B   5     -20.686  28.342  68.367  1.00 29.25           N  
ANISOU 2511  N   GLU B   5     4145   3823   3146    296    442     72       N  
ATOM   2512  CA  GLU B   5     -21.921  28.016  67.678  1.00 27.09           C  
ANISOU 2512  CA  GLU B   5     3847   3496   2951    263    486     91       C  
ATOM   2513  C   GLU B   5     -23.091  28.681  68.377  1.00 31.75           C  
ANISOU 2513  C   GLU B   5     4441   4088   3535    274    529     80       C  
ATOM   2514  O   GLU B   5     -23.188  28.660  69.609  1.00 30.97           O  
ANISOU 2514  O   GLU B   5     4372   4024   3370    319    560     94       O  
ATOM   2515  CB  GLU B   5     -22.150  26.506  67.624  1.00 33.80           C  
ANISOU 2515  CB  GLU B   5     4701   4318   3825    269    538    154       C  
ATOM   2516  CG  GLU B   5     -23.368  26.153  66.760  1.00 34.92           C  
ANISOU 2516  CG  GLU B   5     4808   4404   4056    226    577    164       C  
ATOM   2517  CD  GLU B   5     -23.629  24.663  66.690  1.00 43.20           C  
ANISOU 2517  CD  GLU B   5     5858   5418   5139    227    633    221       C  
ATOM   2518  OE1 GLU B   5     -22.711  23.880  67.017  1.00 42.40           O  
ANISOU 2518  OE1 GLU B   5     5780   5328   5001    255    632    254       O  
ATOM   2519  OE2 GLU B   5     -24.755  24.279  66.308  1.00 35.17           O  
ANISOU 2519  OE2 GLU B   5     4816   4360   4188    200    680    232       O  
ATOM   2520  N   GLY B   6     -23.958  29.288  67.591  1.00 30.03           N  
ANISOU 2520  N   GLY B   6     4192   3837   3383    237    531     56       N  
ATOM   2521  CA  GLY B   6     -25.189  29.831  68.098  1.00 30.24           C  
ANISOU 2521  CA  GLY B   6     4214   3858   3419    244    577     51       C  
ATOM   2522  C   GLY B   6     -26.338  29.118  67.421  1.00 28.01           C  
ANISOU 2522  C   GLY B   6     3899   3528   3216    214    623     81       C  
ATOM   2523  O   GLY B   6     -26.141  28.166  66.649  1.00 29.58           O  
ANISOU 2523  O   GLY B   6     4083   3701   3456    191    622    105       O  
ATOM   2524  N   PRO B   7     -27.561  29.570  67.682  1.00 34.13           N  
ANISOU 2524  N   PRO B   7     4661   4292   4016    214    666     77       N  
ATOM   2525  CA  PRO B   7     -28.724  28.901  67.073  1.00 38.89           C  
ANISOU 2525  CA  PRO B   7     5225   4853   4697    185    712    102       C  
ATOM   2526  C   PRO B   7     -28.699  28.924  65.555  1.00 34.87           C  
ANISOU 2526  C   PRO B   7     4674   4318   4258    137    667     82       C  
ATOM   2527  O   PRO B   7     -29.122  27.946  64.925  1.00 31.97           O  
ANISOU 2527  O   PRO B   7     4282   3921   3946    111    690    104       O  
ATOM   2528  CB  PRO B   7     -29.921  29.692  67.618  1.00 36.60           C  
ANISOU 2528  CB  PRO B   7     4926   4564   4416    196    753     90       C  
ATOM   2529  CG  PRO B   7     -29.385  30.530  68.747  1.00 42.43           C  
ANISOU 2529  CG  PRO B   7     5706   5343   5070    238    743     68       C  
ATOM   2530  CD  PRO B   7     -27.935  30.756  68.469  1.00 35.32           C  
ANISOU 2530  CD  PRO B   7     4824   4466   4130    237    672     44       C  
ATOM   2531  N   ASN B   8     -28.184  30.002  64.950  1.00 29.67           N  
ANISOU 2531  N   ASN B   8     4008   3669   3596    125    606     39       N  
ATOM   2532  CA  ASN B   8     -28.189  30.149  63.503  1.00 30.77           C  
ANISOU 2532  CA  ASN B   8     4108   3788   3795     85    564     21       C  
ATOM   2533  C   ASN B   8     -26.878  30.749  62.992  1.00 28.24           C  
ANISOU 2533  C   ASN B   8     3800   3482   3448     80    495     -8       C  
ATOM   2534  O   ASN B   8     -26.868  31.445  61.976  1.00 26.32           O  
ANISOU 2534  O   ASN B   8     3531   3230   3240     57    457    -33       O  
ATOM   2535  CB  ASN B   8     -29.391  31.001  63.040  1.00 27.54           C  
ANISOU 2535  CB  ASN B   8     3661   3368   3436     71    574      1       C  
ATOM   2536  CG  ASN B   8     -29.505  32.313  63.797  1.00 37.23           C  
ANISOU 2536  CG  ASN B   8     4906   4612   4627     97    573    -26       C  
ATOM   2537  OD1 ASN B   8     -28.687  32.605  64.667  1.00 28.24           O  
ANISOU 2537  OD1 ASN B   8     3807   3497   3424    124    563    -35       O  
ATOM   2538  ND2 ASN B   8     -30.509  33.122  63.455  1.00 33.41           N  
ANISOU 2538  ND2 ASN B   8     4391   4120   4185     92    583    -41       N  
ATOM   2539  N   PHE B   9     -25.761  30.471  63.662  1.00 25.40           N  
ANISOU 2539  N   PHE B   9     3477   3145   3030    102    480     -2       N  
ATOM   2540  CA  PHE B   9     -24.486  31.002  63.203  1.00 23.74           C  
ANISOU 2540  CA  PHE B   9     3274   2948   2798     96    417    -30       C  
ATOM   2541  C   PHE B   9     -23.381  30.147  63.795  1.00 27.50           C  
ANISOU 2541  C   PHE B   9     3782   3446   3222    119    410     -8       C  
ATOM   2542  O   PHE B   9     -23.588  29.398  64.755  1.00 27.40           O  
ANISOU 2542  O   PHE B   9     3792   3443   3177    147    453     25       O  
ATOM   2543  CB  PHE B   9     -24.304  32.484  63.596  1.00 21.67           C  
ANISOU 2543  CB  PHE B   9     3020   2702   2509    108    393    -75       C  
ATOM   2544  CG  PHE B   9     -24.348  32.739  65.102  1.00 22.94           C  
ANISOU 2544  CG  PHE B   9     3216   2895   2605    148    420    -80       C  
ATOM   2545  CD1 PHE B   9     -23.193  32.622  65.877  1.00 31.36           C  
ANISOU 2545  CD1 PHE B   9     4315   3999   3603    173    396    -87       C  
ATOM   2546  CD2 PHE B   9     -25.517  33.121  65.715  1.00 26.22           C  
ANISOU 2546  CD2 PHE B   9     3631   3307   3025    161    468    -79       C  
ATOM   2547  CE1 PHE B   9     -23.207  32.860  67.248  1.00 24.41           C  
ANISOU 2547  CE1 PHE B   9     3465   3154   2654    213    418    -94       C  
ATOM   2548  CE2 PHE B   9     -25.563  33.373  67.100  1.00 29.52           C  
ANISOU 2548  CE2 PHE B   9     4082   3756   3378    200    495    -85       C  
ATOM   2549  CZ  PHE B   9     -24.404  33.238  67.872  1.00 30.62           C  
ANISOU 2549  CZ  PHE B   9     4255   3936   3444    227    469    -93       C  
ATOM   2550  N   TYR B  10     -22.202  30.268  63.203  1.00 23.55           N  
ANISOU 2550  N   TYR B  10     3281   2952   2715    108    356    -25       N  
ATOM   2551  CA  TYR B  10     -21.002  29.615  63.726  1.00 25.26           C  
ANISOU 2551  CA  TYR B  10     3524   3195   2879    132    339    -10       C  
ATOM   2552  C   TYR B  10     -19.868  30.611  63.528  1.00 25.14           C  
ANISOU 2552  C   TYR B  10     3509   3201   2841    127    278    -55       C  
ATOM   2553  O   TYR B  10     -19.388  30.792  62.406  1.00 25.73           O  
ANISOU 2553  O   TYR B  10     3564   3258   2954     98    241    -69       O  
ATOM   2554  CB  TYR B  10     -20.691  28.304  63.006  1.00 22.86           C  
ANISOU 2554  CB  TYR B  10     3212   2868   2607    117    345     27       C  
ATOM   2555  CG  TYR B  10     -19.479  27.669  63.608  1.00 25.46           C  
ANISOU 2555  CG  TYR B  10     3568   3226   2881    148    331     46       C  
ATOM   2556  CD1 TYR B  10     -19.604  26.866  64.724  1.00 23.69           C  
ANISOU 2556  CD1 TYR B  10     3371   3018   2613    188    375     88       C  
ATOM   2557  CD2 TYR B  10     -18.201  27.901  63.097  1.00 24.82           C  
ANISOU 2557  CD2 TYR B  10     3483   3158   2789    141    274     25       C  
ATOM   2558  CE1 TYR B  10     -18.487  26.294  65.327  1.00 29.54           C  
ANISOU 2558  CE1 TYR B  10     4136   3791   3297    224    361    109       C  
ATOM   2559  CE2 TYR B  10     -17.080  27.340  63.690  1.00 25.33           C  
ANISOU 2559  CE2 TYR B  10     3568   3255   2801    173    258     42       C  
ATOM   2560  CZ  TYR B  10     -17.240  26.532  64.805  1.00 30.87           C  
ANISOU 2560  CZ  TYR B  10     4297   3975   3456    216    301     85       C  
ATOM   2561  OH  TYR B  10     -16.153  25.953  65.406  1.00 30.67           O  
ANISOU 2561  OH  TYR B  10     4292   3986   3376    254    287    107       O  
ATOM   2562  N   VAL B  11     -19.459  31.261  64.605  1.00 22.62           N  
ANISOU 2562  N   VAL B  11     3213   2920   2462    157    268    -80       N  
ATOM   2563  CA  VAL B  11     -18.403  32.272  64.500  1.00 22.50           C  
ANISOU 2563  CA  VAL B  11     3195   2924   2428    150    212   -131       C  
ATOM   2564  C   VAL B  11     -17.047  31.599  64.644  1.00 21.65           C  
ANISOU 2564  C   VAL B  11     3097   2846   2282    165    179   -121       C  
ATOM   2565  O   VAL B  11     -16.818  30.891  65.628  1.00 24.33           O  
ANISOU 2565  O   VAL B  11     3460   3219   2564    203    195    -94       O  
ATOM   2566  CB  VAL B  11     -18.593  33.376  65.544  1.00 27.27           C  
ANISOU 2566  CB  VAL B  11     3815   3557   2990    171    215   -174       C  
ATOM   2567  CG1 VAL B  11     -17.410  34.342  65.508  1.00 27.55           C  
ANISOU 2567  CG1 VAL B  11     3847   3612   3010    163    159   -230       C  
ATOM   2568  CG2 VAL B  11     -19.926  34.099  65.326  1.00 26.07           C  
ANISOU 2568  CG2 VAL B  11     3651   3373   2883    157    248   -183       C  
ATOM   2569  N   PRO B  12     -16.115  31.778  63.685  1.00 23.00           N  
ANISOU 2569  N   PRO B  12     3250   3007   2481    139    134   -138       N  
ATOM   2570  CA  PRO B  12     -14.781  31.148  63.785  1.00 25.75           C  
ANISOU 2570  CA  PRO B  12     3603   3384   2796    154    100   -129       C  
ATOM   2571  C   PRO B  12     -13.873  31.920  64.734  1.00 27.04           C  
ANISOU 2571  C   PRO B  12     3776   3600   2900    176     64   -175       C  
ATOM   2572  O   PRO B  12     -12.816  32.437  64.367  1.00 25.53           O  
ANISOU 2572  O   PRO B  12     3570   3418   2712    162     17   -211       O  
ATOM   2573  CB  PRO B  12     -14.290  31.186  62.331  1.00 24.51           C  
ANISOU 2573  CB  PRO B  12     3420   3192   2700    114     72   -135       C  
ATOM   2574  CG  PRO B  12     -14.969  32.378  61.733  1.00 24.77           C  
ANISOU 2574  CG  PRO B  12     3436   3196   2778     85     70   -170       C  
ATOM   2575  CD  PRO B  12     -16.285  32.560  62.441  1.00 27.35           C  
ANISOU 2575  CD  PRO B  12     3774   3520   3098     98    115   -163       C  
ATOM   2576  N   PHE B  13     -14.328  32.036  65.969  1.00 25.58           N  
ANISOU 2576  N   PHE B  13     3614   3448   2658    211     87   -178       N  
ATOM   2577  CA  PHE B  13     -13.637  32.810  66.985  1.00 27.27           C  
ANISOU 2577  CA  PHE B  13     3836   3716   2808    234     56   -229       C  
ATOM   2578  C   PHE B  13     -14.080  32.243  68.316  1.00 25.54           C  
ANISOU 2578  C   PHE B  13     3648   3540   2515    286     92   -199       C  
ATOM   2579  O   PHE B  13     -15.277  32.011  68.515  1.00 27.09           O  
ANISOU 2579  O   PHE B  13     3856   3712   2723    291    145   -169       O  
ATOM   2580  CB  PHE B  13     -13.993  34.297  66.893  1.00 26.06           C  
ANISOU 2580  CB  PHE B  13     3674   3548   2682    208     47   -293       C  
ATOM   2581  CG  PHE B  13     -13.007  35.203  67.579  1.00 25.74           C  
ANISOU 2581  CG  PHE B  13     3630   3553   2596    216      3   -362       C  
ATOM   2582  CD1 PHE B  13     -13.177  35.554  68.905  1.00 29.10           C  
ANISOU 2582  CD1 PHE B  13     4078   4029   2951    251     10   -390       C  
ATOM   2583  CD2 PHE B  13     -11.921  35.716  66.876  1.00 34.12           C  
ANISOU 2583  CD2 PHE B  13     4666   4608   3689    186    -45   -400       C  
ATOM   2584  CE1 PHE B  13     -12.258  36.399  69.552  1.00 38.35           C  
ANISOU 2584  CE1 PHE B  13     5244   5247   4081    256    -34   -463       C  
ATOM   2585  CE2 PHE B  13     -11.009  36.555  67.494  1.00 38.61           C  
ANISOU 2585  CE2 PHE B  13     5228   5218   4224    188    -86   -470       C  
ATOM   2586  CZ  PHE B  13     -11.168  36.894  68.832  1.00 33.25           C  
ANISOU 2586  CZ  PHE B  13     4569   4592   3472    222    -82   -504       C  
ATOM   2587  N   SER B  14     -13.130  32.006  69.207  1.00 27.30           N  
ANISOU 2587  N   SER B  14     3883   3826   2662    325     64   -206       N  
ATOM   2588  CA  SER B  14     -13.463  31.395  70.486  1.00 27.33           C  
ANISOU 2588  CA  SER B  14     3919   3877   2587    382     98   -171       C  
ATOM   2589  C   SER B  14     -14.157  32.377  71.419  1.00 30.06           C  
ANISOU 2589  C   SER B  14     4280   4246   2894    395    115   -217       C  
ATOM   2590  O   SER B  14     -13.771  33.545  71.508  1.00 27.69           O  
ANISOU 2590  O   SER B  14     3969   3962   2592    377     77   -291       O  
ATOM   2591  CB  SER B  14     -12.198  30.887  71.174  1.00 28.68           C  
ANISOU 2591  CB  SER B  14     4096   4119   2682    426     60   -166       C  
ATOM   2592  OG  SER B  14     -12.550  30.452  72.468  1.00 31.76           O  
ANISOU 2592  OG  SER B  14     4519   4561   2988    486     93   -135       O  
ATOM   2593  N   ASN B  15     -15.161  31.899  72.162  1.00 30.00           N  
ANISOU 2593  N   ASN B  15     4299   4242   2856    428    174   -173       N  
ATOM   2594  CA  ASN B  15     -15.774  32.742  73.178  1.00 29.51           C  
ANISOU 2594  CA  ASN B  15     4256   4211   2746    450    193   -214       C  
ATOM   2595  C   ASN B  15     -15.151  32.563  74.565  1.00 27.94           C  
ANISOU 2595  C   ASN B  15     4083   4101   2431    512    180   -220       C  
ATOM   2596  O   ASN B  15     -15.785  32.915  75.567  1.00 27.30           O  
ANISOU 2596  O   ASN B  15     4026   4051   2296    544    211   -233       O  
ATOM   2597  CB  ASN B  15     -17.286  32.510  73.277  1.00 30.57           C  
ANISOU 2597  CB  ASN B  15     4403   4303   2911    451    268   -172       C  
ATOM   2598  CG  ASN B  15     -18.013  33.736  73.804  1.00 31.95           C  
ANISOU 2598  CG  ASN B  15     4582   4480   3076    448    282   -231       C  
ATOM   2599  OD1 ASN B  15     -17.510  34.853  73.698  1.00 28.99           O  
ANISOU 2599  OD1 ASN B  15     4196   4114   2707    426    237   -305       O  
ATOM   2600  ND2 ASN B  15     -19.195  33.541  74.369  1.00 30.99           N  
ANISOU 2600  ND2 ASN B  15     4479   4349   2946    469    347   -198       N  
ATOM   2601  N   LYS B  16     -13.917  32.074  74.648  1.00 30.47           N  
ANISOU 2601  N   LYS B  16     4398   4467   2711    533    133   -215       N  
ATOM   2602  CA  LYS B  16     -13.314  31.865  75.962  1.00 30.60           C  
ANISOU 2602  CA  LYS B  16     4438   4578   2612    598    118   -218       C  
ATOM   2603  C   LYS B  16     -13.132  33.171  76.716  1.00 38.16           C  
ANISOU 2603  C   LYS B  16     5395   5585   3518    600     84   -314       C  
ATOM   2604  O   LYS B  16     -13.043  33.152  77.948  1.00 41.37           O  
ANISOU 2604  O   LYS B  16     5826   6068   3824    657     86   -322       O  
ATOM   2605  CB  LYS B  16     -11.974  31.127  75.814  1.00 31.02           C  
ANISOU 2605  CB  LYS B  16     4478   4671   2638    619     69   -196       C  
ATOM   2606  CG  LYS B  16     -10.885  31.890  75.107  1.00 40.58           C  
ANISOU 2606  CG  LYS B  16     5650   5882   3884    574     -5   -268       C  
ATOM   2607  CD  LYS B  16      -9.655  31.008  74.863  1.00 46.44           C  
ANISOU 2607  CD  LYS B  16     6379   6656   4611    595    -44   -233       C  
ATOM   2608  CE  LYS B  16      -8.702  31.687  73.898  1.00 49.96           C  
ANISOU 2608  CE  LYS B  16     6783   7083   5119    539   -106   -294       C  
ATOM   2609  NZ  LYS B  16      -7.389  30.979  73.789  1.00 59.06           N  
ANISOU 2609  NZ  LYS B  16     7917   8278   6246    563   -152   -274       N  
ATOM   2610  N   THR B  17     -13.098  34.308  76.014  1.00 34.02           N  
ANISOU 2610  N   THR B  17     4845   5020   3063    542     56   -387       N  
ATOM   2611  CA  THR B  17     -13.025  35.604  76.683  1.00 31.74           C  
ANISOU 2611  CA  THR B  17     4556   4766   2740    537     32   -483       C  
ATOM   2612  C   THR B  17     -14.355  36.348  76.720  1.00 40.02           C  
ANISOU 2612  C   THR B  17     5616   5764   3826    518     86   -500       C  
ATOM   2613  O   THR B  17     -14.403  37.470  77.228  1.00 36.63           O  
ANISOU 2613  O   THR B  17     5187   5352   3378    512     74   -582       O  
ATOM   2614  CB  THR B  17     -11.957  36.480  76.025  1.00 40.68           C  
ANISOU 2614  CB  THR B  17     5650   5892   3916    489    -35   -562       C  
ATOM   2615  OG1 THR B  17     -12.313  36.732  74.660  1.00 34.57           O  
ANISOU 2615  OG1 THR B  17     4853   5024   3257    429    -24   -551       O  
ATOM   2616  CG2 THR B  17     -10.600  35.775  76.074  1.00 42.09           C  
ANISOU 2616  CG2 THR B  17     5813   6128   4051    511    -91   -550       C  
ATOM   2617  N   GLY B  18     -15.435  35.759  76.211  1.00 31.81           N  
ANISOU 2617  N   GLY B  18     4584   4662   2842    510    145   -429       N  
ATOM   2618  CA  GLY B  18     -16.745  36.352  76.399  1.00 27.54           C  
ANISOU 2618  CA  GLY B  18     4054   4083   2327    503    201   -437       C  
ATOM   2619  C   GLY B  18     -17.119  37.478  75.453  1.00 29.91           C  
ANISOU 2619  C   GLY B  18     4328   4313   2723    443    195   -488       C  
ATOM   2620  O   GLY B  18     -18.155  38.117  75.674  1.00 34.62           O  
ANISOU 2620  O   GLY B  18     4932   4882   3338    440    238   -505       O  
ATOM   2621  N   VAL B  19     -16.334  37.725  74.398  1.00 31.10           N  
ANISOU 2621  N   VAL B  19     4447   4432   2936    399    148   -509       N  
ATOM   2622  CA  VAL B  19     -16.583  38.874  73.522  1.00 31.89           C  
ANISOU 2622  CA  VAL B  19     4524   4470   3124    346    142   -559       C  
ATOM   2623  C   VAL B  19     -17.456  38.546  72.317  1.00 34.09           C  
ANISOU 2623  C   VAL B  19     4786   4672   3496    314    175   -501       C  
ATOM   2624  O   VAL B  19     -17.893  39.476  71.620  1.00 37.73           O  
ANISOU 2624  O   VAL B  19     5229   5078   4027    279    181   -531       O  
ATOM   2625  CB  VAL B  19     -15.275  39.504  72.983  1.00 28.40           C  
ANISOU 2625  CB  VAL B  19     4054   4031   2706    313     76   -620       C  
ATOM   2626  CG1 VAL B  19     -14.413  40.026  74.153  1.00 38.70           C  
ANISOU 2626  CG1 VAL B  19     5367   5412   3925    338     38   -697       C  
ATOM   2627  CG2 VAL B  19     -14.494  38.523  72.114  1.00 31.21           C  
ANISOU 2627  CG2 VAL B  19     4393   4379   3086    301     47   -568       C  
ATOM   2628  N   VAL B  20     -17.720  37.268  72.033  1.00 28.14           N  
ANISOU 2628  N   VAL B  20     4036   3911   2746    326    197   -421       N  
ATOM   2629  CA  VAL B  20     -18.407  36.938  70.787  1.00 27.62           C  
ANISOU 2629  CA  VAL B  20     3949   3777   2770    290    218   -376       C  
ATOM   2630  C   VAL B  20     -19.865  37.366  70.865  1.00 31.84           C  
ANISOU 2630  C   VAL B  20     4485   4275   3337    289    275   -368       C  
ATOM   2631  O   VAL B  20     -20.547  37.148  71.878  1.00 33.18           O  
ANISOU 2631  O   VAL B  20     4679   4471   3459    325    318   -353       O  
ATOM   2632  CB  VAL B  20     -18.267  35.447  70.448  1.00 26.81           C  
ANISOU 2632  CB  VAL B  20     3848   3673   2667    300    228   -299       C  
ATOM   2633  CG1 VAL B  20     -19.075  35.091  69.165  1.00 24.00           C  
ANISOU 2633  CG1 VAL B  20     3467   3250   2403    262    251   -258       C  
ATOM   2634  CG2 VAL B  20     -16.800  35.097  70.240  1.00 26.57           C  
ANISOU 2634  CG2 VAL B  20     3810   3673   2612    299    170   -308       C  
ATOM   2635  N   ARG B  21     -20.347  37.990  69.789  1.00 31.21           N  
ANISOU 2635  N   ARG B  21     4379   4139   3342    250    276   -377       N  
ATOM   2636  CA  ARG B  21     -21.737  38.389  69.654  1.00 29.11           C  
ANISOU 2636  CA  ARG B  21     4105   3834   3120    246    326   -366       C  
ATOM   2637  C   ARG B  21     -22.277  37.893  68.324  1.00 30.85           C  
ANISOU 2637  C   ARG B  21     4295   4005   3420    214    334   -319       C  
ATOM   2638  O   ARG B  21     -21.535  37.771  67.334  1.00 26.20           O  
ANISOU 2638  O   ARG B  21     3689   3401   2866    186    293   -318       O  
ATOM   2639  CB  ARG B  21     -21.904  39.913  69.757  1.00 35.42           C  
ANISOU 2639  CB  ARG B  21     4900   4617   3940    235    324   -433       C  
ATOM   2640  CG  ARG B  21     -21.488  40.457  71.125  1.00 39.51           C  
ANISOU 2640  CG  ARG B  21     5448   5187   4378    266    320   -489       C  
ATOM   2641  CD  ARG B  21     -22.313  41.641  71.560  1.00 54.79           C  
ANISOU 2641  CD  ARG B  21     7388   7104   6328    270    354   -535       C  
ATOM   2642  NE  ARG B  21     -21.775  42.893  71.042  1.00 71.66           N  
ANISOU 2642  NE  ARG B  21     9508   9210   8509    240    324   -599       N  
ATOM   2643  CZ  ARG B  21     -22.299  44.087  71.280  1.00 63.50           C  
ANISOU 2643  CZ  ARG B  21     8475   8152   7500    238    348   -649       C  
ATOM   2644  NH1 ARG B  21     -23.388  44.228  72.018  1.00 68.91           N  
ANISOU 2644  NH1 ARG B  21     9176   8840   8167    265    401   -643       N  
ATOM   2645  NH2 ARG B  21     -21.717  45.166  70.764  1.00 60.82           N  
ANISOU 2645  NH2 ARG B  21     8122   7781   7208    210    323   -704       N  
ATOM   2646  N   SER B  22     -23.575  37.602  68.320  1.00 25.14           N  
ANISOU 2646  N   SER B  22     3565   3260   2726    218    386   -284       N  
ATOM   2647  CA  SER B  22     -24.224  37.117  67.107  1.00 25.04           C  
ANISOU 2647  CA  SER B  22     3521   3206   2788    190    394   -244       C  
ATOM   2648  C   SER B  22     -23.996  38.088  65.949  1.00 26.22           C  
ANISOU 2648  C   SER B  22     3644   3322   2997    157    359   -274       C  
ATOM   2649  O   SER B  22     -24.150  39.307  66.111  1.00 27.11           O  
ANISOU 2649  O   SER B  22     3756   3424   3119    158    360   -317       O  
ATOM   2650  CB  SER B  22     -25.729  36.940  67.322  1.00 28.20           C  
ANISOU 2650  CB  SER B  22     3911   3588   3215    198    456   -215       C  
ATOM   2651  OG  SER B  22     -26.372  36.710  66.072  1.00 29.89           O  
ANISOU 2651  OG  SER B  22     4087   3764   3505    168    457   -190       O  
ATOM   2652  N   PRO B  23     -23.674  37.578  64.758  1.00 23.65           N  
ANISOU 2652  N   PRO B  23     3295   2977   2714    130    332   -251       N  
ATOM   2653  CA  PRO B  23     -23.545  38.438  63.575  1.00 24.44           C  
ANISOU 2653  CA  PRO B  23     3369   3045   2871    103    304   -270       C  
ATOM   2654  C   PRO B  23     -24.867  38.979  63.075  1.00 26.46           C  
ANISOU 2654  C   PRO B  23     3600   3272   3183     99    336   -261       C  
ATOM   2655  O   PRO B  23     -24.877  39.697  62.071  1.00 25.98           O  
ANISOU 2655  O   PRO B  23     3516   3186   3169     82    318   -270       O  
ATOM   2656  CB  PRO B  23     -22.924  37.503  62.527  1.00 23.54           C  
ANISOU 2656  CB  PRO B  23     3240   2925   2778     81    274   -241       C  
ATOM   2657  CG  PRO B  23     -23.411  36.122  62.937  1.00 24.37           C  
ANISOU 2657  CG  PRO B  23     3352   3042   2867     91    306   -195       C  
ATOM   2658  CD  PRO B  23     -23.384  36.164  64.467  1.00 21.90           C  
ANISOU 2658  CD  PRO B  23     3073   2761   2487    126    330   -206       C  
ATOM   2659  N   PHE B  24     -25.981  38.617  63.702  1.00 24.66           N  
ANISOU 2659  N   PHE B  24     3371   3047   2950    116    383   -240       N  
ATOM   2660  CA  PHE B  24     -27.261  39.264  63.426  1.00 23.23           C  
ANISOU 2660  CA  PHE B  24     3165   2843   2816    118    416   -237       C  
ATOM   2661  C   PHE B  24     -27.598  40.306  64.473  1.00 33.46           C  
ANISOU 2661  C   PHE B  24     4481   4143   4089    142    444   -273       C  
ATOM   2662  O   PHE B  24     -28.674  40.913  64.411  1.00 29.62           O  
ANISOU 2662  O   PHE B  24     3978   3639   3638    150    476   -272       O  
ATOM   2663  CB  PHE B  24     -28.374  38.204  63.353  1.00 23.95           C  
ANISOU 2663  CB  PHE B  24     3236   2933   2930    117    455   -192       C  
ATOM   2664  CG  PHE B  24     -28.129  37.163  62.305  1.00 27.55           C  
ANISOU 2664  CG  PHE B  24     3670   3383   3413     91    431   -163       C  
ATOM   2665  CD1 PHE B  24     -28.002  37.533  60.963  1.00 25.50           C  
ANISOU 2665  CD1 PHE B  24     3382   3108   3200     68    396   -166       C  
ATOM   2666  CD2 PHE B  24     -28.002  35.820  62.642  1.00 29.71           C  
ANISOU 2666  CD2 PHE B  24     3954   3667   3667     90    447   -132       C  
ATOM   2667  CE1 PHE B  24     -27.765  36.574  59.970  1.00 27.38           C  
ANISOU 2667  CE1 PHE B  24     3599   3342   3460     44    373   -144       C  
ATOM   2668  CE2 PHE B  24     -27.763  34.858  61.651  1.00 29.74           C  
ANISOU 2668  CE2 PHE B  24     3939   3662   3700     65    427   -110       C  
ATOM   2669  CZ  PHE B  24     -27.647  35.236  60.324  1.00 28.14           C  
ANISOU 2669  CZ  PHE B  24     3706   3446   3540     41    389   -118       C  
ATOM   2670  N   GLU B  25     -26.713  40.529  65.439  1.00 25.36           N  
ANISOU 2670  N   GLU B  25     3491   3142   3004    156    432   -306       N  
ATOM   2671  CA  GLU B  25     -27.033  41.468  66.506  1.00 28.68           C  
ANISOU 2671  CA  GLU B  25     3933   3570   3396    180    460   -346       C  
ATOM   2672  C   GLU B  25     -26.066  42.630  66.625  1.00 36.27           C  
ANISOU 2672  C   GLU B  25     4906   4527   4348    174    428   -407       C  
ATOM   2673  O   GLU B  25     -26.489  43.713  67.016  1.00 32.39           O  
ANISOU 2673  O   GLU B  25     4419   4021   3868    184    451   -444       O  
ATOM   2674  CB  GLU B  25     -27.083  40.741  67.854  1.00 35.29           C  
ANISOU 2674  CB  GLU B  25     4802   4447   4160    210    488   -337       C  
ATOM   2675  CG  GLU B  25     -28.129  39.657  67.896  1.00 38.19           C  
ANISOU 2675  CG  GLU B  25     5158   4812   4540    217    534   -279       C  
ATOM   2676  CD  GLU B  25     -28.161  38.940  69.239  1.00 49.50           C  
ANISOU 2676  CD  GLU B  25     6625   6283   5899    251    568   -264       C  
ATOM   2677  OE1 GLU B  25     -27.368  39.305  70.144  1.00 43.84           O  
ANISOU 2677  OE1 GLU B  25     5941   5601   5115    271    552   -301       O  
ATOM   2678  OE2 GLU B  25     -28.977  38.004  69.375  1.00 49.85           O  
ANISOU 2678  OE2 GLU B  25     6662   6324   5953    258    612   -214       O  
ATOM   2679  N   ALA B  26     -24.786  42.448  66.317  1.00 28.97           N  
ANISOU 2679  N   ALA B  26     3987   3614   3408    158    379   -421       N  
ATOM   2680  CA  ALA B  26     -23.862  43.533  66.610  1.00 32.15           C  
ANISOU 2680  CA  ALA B  26     4401   4017   3800    153    353   -487       C  
ATOM   2681  C   ALA B  26     -22.679  43.467  65.665  1.00 27.62           C  
ANISOU 2681  C   ALA B  26     3813   3434   3247    125    301   -491       C  
ATOM   2682  O   ALA B  26     -22.329  42.381  65.184  1.00 23.93           O  
ANISOU 2682  O   ALA B  26     3339   2979   2773    117    281   -449       O  
ATOM   2683  CB  ALA B  26     -23.373  43.472  68.069  1.00 35.36           C  
ANISOU 2683  CB  ALA B  26     4841   4472   4122    178    353   -525       C  
ATOM   2684  N   PRO B  27     -22.010  44.595  65.428  1.00 28.94           N  
ANISOU 2684  N   PRO B  27     3976   3578   3440    109    282   -542       N  
ATOM   2685  CA  PRO B  27     -20.817  44.601  64.577  1.00 31.42           C  
ANISOU 2685  CA  PRO B  27     4277   3884   3776     83    236   -550       C  
ATOM   2686  C   PRO B  27     -19.770  43.628  65.090  1.00 27.42           C  
ANISOU 2686  C   PRO B  27     3784   3428   3207     87    200   -550       C  
ATOM   2687  O   PRO B  27     -19.562  43.491  66.302  1.00 30.76           O  
ANISOU 2687  O   PRO B  27     4229   3893   3564    108    201   -577       O  
ATOM   2688  CB  PRO B  27     -20.309  46.050  64.687  1.00 32.71           C  
ANISOU 2688  CB  PRO B  27     4440   4020   3968     71    233   -618       C  
ATOM   2689  CG  PRO B  27     -21.456  46.839  65.149  1.00 37.04           C  
ANISOU 2689  CG  PRO B  27     4995   4547   4533     88    281   -631       C  
ATOM   2690  CD  PRO B  27     -22.320  45.937  65.965  1.00 35.82           C  
ANISOU 2690  CD  PRO B  27     4855   4429   4326    116    307   -598       C  
ATOM   2691  N   GLN B  28     -19.063  43.008  64.155  1.00 30.37           N  
ANISOU 2691  N   GLN B  28     4142   3797   3599     68    168   -521       N  
ATOM   2692  CA  GLN B  28     -18.115  41.933  64.455  1.00 24.78           C  
ANISOU 2692  CA  GLN B  28     3442   3132   2839     73    135   -507       C  
ATOM   2693  C   GLN B  28     -16.687  42.442  64.611  1.00 22.42           C  
ANISOU 2693  C   GLN B  28     3141   2850   2528     60     92   -562       C  
ATOM   2694  O   GLN B  28     -15.723  41.776  64.229  1.00 23.25           O  
ANISOU 2694  O   GLN B  28     3238   2971   2623     52     57   -549       O  
ATOM   2695  CB  GLN B  28     -18.211  40.874  63.361  1.00 24.85           C  
ANISOU 2695  CB  GLN B  28     3436   3127   2877     61    129   -444       C  
ATOM   2696  CG  GLN B  28     -19.614  40.244  63.257  1.00 21.61           C  
ANISOU 2696  CG  GLN B  28     3024   2705   2480     72    172   -393       C  
ATOM   2697  CD  GLN B  28     -19.941  39.348  64.452  1.00 25.70           C  
ANISOU 2697  CD  GLN B  28     3567   3264   2935    102    195   -373       C  
ATOM   2698  OE1 GLN B  28     -19.393  38.250  64.577  1.00 27.50           O  
ANISOU 2698  OE1 GLN B  28     3802   3516   3130    110    183   -344       O  
ATOM   2699  NE2 GLN B  28     -20.831  39.813  65.331  1.00 25.11           N  
ANISOU 2699  NE2 GLN B  28     3505   3194   2842    123    233   -387       N  
ATOM   2700  N   TYR B  29     -16.530  43.642  65.170  1.00 29.40           N  
ANISOU 2700  N   TYR B  29     4028   3729   3414     57     94   -629       N  
ATOM   2701  CA  TYR B  29     -15.222  44.261  65.349  1.00 31.66           C  
ANISOU 2701  CA  TYR B  29     4306   4027   3695     41     55   -692       C  
ATOM   2702  C   TYR B  29     -14.335  43.534  66.348  1.00 38.07           C  
ANISOU 2702  C   TYR B  29     5129   4910   4425     62     21   -710       C  
ATOM   2703  O   TYR B  29     -13.146  43.859  66.445  1.00 33.84           O  
ANISOU 2703  O   TYR B  29     4582   4393   3883     48    -18   -759       O  
ATOM   2704  CB  TYR B  29     -15.396  45.704  65.819  1.00 33.30           C  
ANISOU 2704  CB  TYR B  29     4516   4211   3926     34     73   -764       C  
ATOM   2705  CG  TYR B  29     -16.167  46.570  64.857  1.00 32.99           C  
ANISOU 2705  CG  TYR B  29     4464   4101   3969     17    107   -751       C  
ATOM   2706  CD1 TYR B  29     -15.950  46.495  63.477  1.00 33.37           C  
ANISOU 2706  CD1 TYR B  29     4491   4109   4079     -5     99   -710       C  
ATOM   2707  CD2 TYR B  29     -17.084  47.467  65.325  1.00 33.20           C  
ANISOU 2707  CD2 TYR B  29     4500   4103   4011     27    148   -778       C  
ATOM   2708  CE1 TYR B  29     -16.659  47.319  62.592  1.00 37.55           C  
ANISOU 2708  CE1 TYR B  29     5009   4578   4681    -14    130   -694       C  
ATOM   2709  CE2 TYR B  29     -17.794  48.275  64.471  1.00 36.94           C  
ANISOU 2709  CE2 TYR B  29     4961   4513   4560     18    180   -762       C  
ATOM   2710  CZ  TYR B  29     -17.582  48.203  63.113  1.00 39.63           C  
ANISOU 2710  CZ  TYR B  29     5280   4818   4958     -1    171   -719       C  
ATOM   2711  OH  TYR B  29     -18.318  49.035  62.314  1.00 34.30           O  
ANISOU 2711  OH  TYR B  29     4594   4086   4352     -3    204   -700       O  
ATOM   2712  N   TYR B  30     -14.873  42.586  67.112  1.00 29.93           N  
ANISOU 2712  N   TYR B  30     4120   3919   3331     96     37   -671       N  
ATOM   2713  CA  TYR B  30     -14.007  41.818  67.994  1.00 33.66           C  
ANISOU 2713  CA  TYR B  30     4604   4462   3723    122      6   -677       C  
ATOM   2714  C   TYR B  30     -13.136  40.828  67.231  1.00 26.56           C  
ANISOU 2714  C   TYR B  30     3690   3569   2832    114    -27   -632       C  
ATOM   2715  O   TYR B  30     -12.164  40.339  67.798  1.00 37.19           O  
ANISOU 2715  O   TYR B  30     5037   4970   4122    131    -62   -644       O  
ATOM   2716  CB  TYR B  30     -14.833  41.098  69.063  1.00 35.75           C  
ANISOU 2716  CB  TYR B  30     4899   4767   3918    166     39   -643       C  
ATOM   2717  CG  TYR B  30     -15.769  40.092  68.463  1.00 29.09           C  
ANISOU 2717  CG  TYR B  30     4058   3894   3100    170     75   -558       C  
ATOM   2718  CD1 TYR B  30     -17.063  40.455  68.092  1.00 31.08           C  
ANISOU 2718  CD1 TYR B  30     4309   4098   3402    162    120   -539       C  
ATOM   2719  CD2 TYR B  30     -15.370  38.782  68.263  1.00 26.35           C  
ANISOU 2719  CD2 TYR B  30     3713   3567   2732    182     64   -499       C  
ATOM   2720  CE1 TYR B  30     -17.933  39.528  67.525  1.00 29.26           C  
ANISOU 2720  CE1 TYR B  30     4076   3843   3199    163    152   -467       C  
ATOM   2721  CE2 TYR B  30     -16.233  37.846  67.690  1.00 33.21           C  
ANISOU 2721  CE2 TYR B  30     4583   4406   3631    182    100   -428       C  
ATOM   2722  CZ  TYR B  30     -17.513  38.236  67.326  1.00 25.47           C  
ANISOU 2722  CZ  TYR B  30     3598   3380   2700    171    142   -415       C  
ATOM   2723  OH  TYR B  30     -18.376  37.318  66.758  1.00 33.71           O  
ANISOU 2723  OH  TYR B  30     4636   4397   3776    168    175   -350       O  
ATOM   2724  N   LEU B  31     -13.457  40.485  65.974  1.00 26.14           N  
ANISOU 2724  N   LEU B  31     3623   3465   2844     90    -16   -581       N  
ATOM   2725  CA  LEU B  31     -12.639  39.520  65.250  1.00 33.53           C  
ANISOU 2725  CA  LEU B  31     4547   4406   3787     83    -44   -541       C  
ATOM   2726  C   LEU B  31     -11.902  40.114  64.053  1.00 30.01           C  
ANISOU 2726  C   LEU B  31     4074   3920   3411     44    -69   -559       C  
ATOM   2727  O   LEU B  31     -11.240  39.370  63.321  1.00 26.84           O  
ANISOU 2727  O   LEU B  31     3659   3516   3021     35    -89   -526       O  
ATOM   2728  CB  LEU B  31     -13.487  38.326  64.809  1.00 36.96           C  
ANISOU 2728  CB  LEU B  31     4990   4825   4230     93    -13   -462       C  
ATOM   2729  CG  LEU B  31     -14.791  38.590  64.063  1.00 27.19           C  
ANISOU 2729  CG  LEU B  31     3747   3534   3051     78     27   -435       C  
ATOM   2730  CD1 LEU B  31     -14.535  39.140  62.658  1.00 32.70           C  
ANISOU 2730  CD1 LEU B  31     4419   4183   3823     41     12   -438       C  
ATOM   2731  CD2 LEU B  31     -15.554  37.291  64.014  1.00 28.23           C  
ANISOU 2731  CD2 LEU B  31     3887   3665   3173     93     57   -367       C  
ATOM   2732  N   ALA B  32     -12.037  41.417  63.806  1.00 27.35           N  
ANISOU 2732  N   ALA B  32     3726   3546   3120     21    -62   -608       N  
ATOM   2733  CA  ALA B  32     -11.290  42.080  62.739  1.00 30.93           C  
ANISOU 2733  CA  ALA B  32     4154   3960   3639    -14    -80   -627       C  
ATOM   2734  C   ALA B  32     -11.414  43.580  62.936  1.00 32.20           C  
ANISOU 2734  C   ALA B  32     4309   4089   3836    -31    -67   -692       C  
ATOM   2735  O   ALA B  32     -12.399  44.067  63.494  1.00 32.68           O  
ANISOU 2735  O   ALA B  32     4386   4142   3890    -18    -35   -704       O  
ATOM   2736  CB  ALA B  32     -11.800  41.708  61.353  1.00 25.99           C  
ANISOU 2736  CB  ALA B  32     3519   3288   3070    -30    -64   -566       C  
ATOM   2737  N  AGLU B  33     -10.415  44.309  62.446  0.43 34.34           N  
ANISOU 2737  N  AGLU B  33     4558   4340   4150    -60    -88   -733       N  
ATOM   2738  N  BGLU B  33     -10.420  44.307  62.428  0.57 34.29           N  
ANISOU 2738  N  BGLU B  33     4552   4333   4145    -60    -88   -732       N  
ATOM   2739  CA AGLU B  33     -10.432  45.750  62.645  0.43 34.08           C  
ANISOU 2739  CA AGLU B  33     4518   4272   4159    -78    -72   -800       C  
ATOM   2740  CA BGLU B  33     -10.396  45.754  62.585  0.57 34.08           C  
ANISOU 2740  CA BGLU B  33     4517   4270   4161    -79    -73   -799       C  
ATOM   2741  C  AGLU B  33     -11.418  46.418  61.685  0.43 30.40           C  
ANISOU 2741  C  AGLU B  33     4051   3736   3763    -87    -30   -768       C  
ATOM   2742  C  BGLU B  33     -11.442  46.407  61.682  0.57 30.36           C  
ANISOU 2742  C  BGLU B  33     4047   3732   3758    -87    -29   -767       C  
ATOM   2743  O  AGLU B  33     -11.701  45.885  60.607  0.43 28.80           O  
ANISOU 2743  O  AGLU B  33     3843   3512   3589    -90    -24   -704       O  
ATOM   2744  O  BGLU B  33     -11.783  45.862  60.627  0.57 28.77           O  
ANISOU 2744  O  BGLU B  33     3840   3507   3583    -89    -22   -702       O  
ATOM   2745  CB AGLU B  33      -9.037  46.329  62.439  0.43 39.85           C  
ANISOU 2745  CB AGLU B  33     5222   4999   4920   -107   -104   -856       C  
ATOM   2746  CB BGLU B  33      -9.019  46.295  62.225  0.57 40.07           C  
ANISOU 2746  CB BGLU B  33     5248   5020   4957   -110   -103   -848       C  
ATOM   2747  CG AGLU B  33      -8.000  45.788  63.411  0.43 42.79           C  
ANISOU 2747  CG AGLU B  33     5589   5444   5223    -96   -150   -896       C  
ATOM   2748  CG BGLU B  33      -7.867  45.539  62.854  0.57 45.19           C  
ANISOU 2748  CG BGLU B  33     5888   5736   5546   -102   -152   -869       C  
ATOM   2749  CD AGLU B  33      -6.726  46.615  63.423  0.43 48.26           C  
ANISOU 2749  CD AGLU B  33     6252   6135   5951   -128   -177   -972       C  
ATOM   2750  CD BGLU B  33      -7.311  46.257  64.058  0.57 46.63           C  
ANISOU 2750  CD BGLU B  33     6065   5956   5695   -103   -172   -962       C  
ATOM   2751  OE1AGLU B  33      -6.819  47.861  63.367  0.43 44.00           O  
ANISOU 2751  OE1AGLU B  33     5704   5547   5466   -152   -154  -1027       O  
ATOM   2752  OE1BGLU B  33      -8.052  46.426  65.047  0.57 48.73           O  
ANISOU 2752  OE1BGLU B  33     6355   6247   5915    -80   -156   -984       O  
ATOM   2753  OE2AGLU B  33      -5.631  46.018  63.494  0.43 53.68           O  
ANISOU 2753  OE2AGLU B  33     6919   6864   6611   -129   -220   -979       O  
ATOM   2754  OE2BGLU B  33      -6.132  46.669  64.006  0.57 53.08           O  
ANISOU 2754  OE2BGLU B  33     6854   6780   6534   -128   -202  -1015       O  
ATOM   2755  N   PRO B  34     -11.940  47.593  62.053  1.00 29.30           N  
ANISOU 2755  N   PRO B  34     3916   3564   3652    -91      1   -813       N  
ATOM   2756  CA  PRO B  34     -12.928  48.262  61.179  1.00 31.92           C  
ANISOU 2756  CA  PRO B  34     4246   3832   4049    -93     44   -779       C  
ATOM   2757  C   PRO B  34     -12.410  48.515  59.762  1.00 24.72           C  
ANISOU 2757  C   PRO B  34     3314   2874   3206   -116     42   -750       C  
ATOM   2758  O   PRO B  34     -13.194  48.448  58.805  1.00 26.73           O  
ANISOU 2758  O   PRO B  34     3565   3097   3494   -110     65   -690       O  
ATOM   2759  CB  PRO B  34     -13.227  49.568  61.939  1.00 32.55           C  
ANISOU 2759  CB  PRO B  34     4332   3885   4149    -95     73   -849       C  
ATOM   2760  CG  PRO B  34     -12.911  49.231  63.393  1.00 35.61           C  
ANISOU 2760  CG  PRO B  34     4734   4339   4456    -81     50   -902       C  
ATOM   2761  CD  PRO B  34     -11.700  48.355  63.299  1.00 34.32           C  
ANISOU 2761  CD  PRO B  34     4559   4221   4260    -89     -1   -898       C  
ATOM   2762  N   TRP B  35     -11.109  48.750  59.584  1.00 28.74           N  
ANISOU 2762  N   TRP B  35     3805   3382   3734   -141     16   -787       N  
ATOM   2763  CA  TRP B  35     -10.595  48.984  58.235  1.00 29.31           C  
ANISOU 2763  CA  TRP B  35     3858   3410   3870   -161     19   -755       C  
ATOM   2764  C   TRP B  35     -10.684  47.737  57.353  1.00 32.99           C  
ANISOU 2764  C   TRP B  35     4323   3896   4317   -152      2   -679       C  
ATOM   2765  O   TRP B  35     -10.794  47.849  56.121  1.00 27.96           O  
ANISOU 2765  O   TRP B  35     3676   3222   3725   -158     15   -633       O  
ATOM   2766  CB  TRP B  35      -9.153  49.493  58.295  1.00 35.01           C  
ANISOU 2766  CB  TRP B  35     4558   4126   4618   -191     -4   -816       C  
ATOM   2767  CG  TRP B  35      -8.118  48.476  58.770  1.00 29.40           C  
ANISOU 2767  CG  TRP B  35     3840   3480   3849   -192    -55   -828       C  
ATOM   2768  CD1 TRP B  35      -7.630  48.355  60.038  1.00 40.95           C  
ANISOU 2768  CD1 TRP B  35     5304   4997   5256   -188    -84   -889       C  
ATOM   2769  CD2 TRP B  35      -7.441  47.475  57.981  1.00 28.92           C  
ANISOU 2769  CD2 TRP B  35     3768   3438   3781   -195    -82   -779       C  
ATOM   2770  NE1 TRP B  35      -6.707  47.340  60.093  1.00 38.88           N  
ANISOU 2770  NE1 TRP B  35     5032   4787   4952   -185   -127   -877       N  
ATOM   2771  CE2 TRP B  35      -6.575  46.781  58.852  1.00 40.92           C  
ANISOU 2771  CE2 TRP B  35     5283   5022   5241   -190   -125   -811       C  
ATOM   2772  CE3 TRP B  35      -7.484  47.099  56.634  1.00 40.00           C  
ANISOU 2772  CE3 TRP B  35     5166   4813   5220   -199    -74   -713       C  
ATOM   2773  CZ2 TRP B  35      -5.769  45.737  58.426  1.00 43.49           C  
ANISOU 2773  CZ2 TRP B  35     5599   5379   5548   -189   -157   -776       C  
ATOM   2774  CZ3 TRP B  35      -6.678  46.046  56.219  1.00 55.07           C  
ANISOU 2774  CZ3 TRP B  35     7065   6753   7106   -200   -106   -683       C  
ATOM   2775  CH2 TRP B  35      -5.828  45.386  57.107  1.00 45.85           C  
ANISOU 2775  CH2 TRP B  35     5893   5644   5885   -195   -146   -714       C  
ATOM   2776  N   GLN B  36     -10.610  46.546  57.952  1.00 26.23           N  
ANISOU 2776  N   GLN B  36     3476   3097   3392   -138    -26   -664       N  
ATOM   2777  CA  GLN B  36     -10.792  45.322  57.185  1.00 23.62           C  
ANISOU 2777  CA  GLN B  36     3146   2783   3046   -130    -37   -595       C  
ATOM   2778  C   GLN B  36     -12.223  45.199  56.645  1.00 20.67           C  
ANISOU 2778  C   GLN B  36     2780   2388   2686   -114     -5   -542       C  
ATOM   2779  O   GLN B  36     -12.418  44.839  55.473  1.00 24.44           O  
ANISOU 2779  O   GLN B  36     3248   2849   3189   -117     -3   -492       O  
ATOM   2780  CB  GLN B  36     -10.448  44.107  58.066  1.00 28.04           C  
ANISOU 2780  CB  GLN B  36     3716   3405   3532   -114    -66   -592       C  
ATOM   2781  CG  GLN B  36      -9.055  44.162  58.703  1.00 35.81           C  
ANISOU 2781  CG  GLN B  36     4690   4423   4495   -123   -103   -645       C  
ATOM   2782  CD  GLN B  36      -8.785  42.936  59.563  1.00 36.25           C  
ANISOU 2782  CD  GLN B  36     4757   4543   4474    -99   -129   -633       C  
ATOM   2783  OE1 GLN B  36      -8.768  43.019  60.783  1.00 39.56           O  
ANISOU 2783  OE1 GLN B  36     5187   5001   4842    -83   -137   -672       O  
ATOM   2784  NE2 GLN B  36      -8.609  41.790  58.922  1.00 48.71           N  
ANISOU 2784  NE2 GLN B  36     6334   6131   6044    -94   -139   -576       N  
ATOM   2785  N   PHE B  37     -13.226  45.549  57.461  1.00 20.83           N  
ANISOU 2785  N   PHE B  37     2814   2411   2691    -98     20   -555       N  
ATOM   2786  CA  PHE B  37     -14.593  45.543  56.950  1.00 22.24           C  
ANISOU 2786  CA  PHE B  37     2993   2568   2888    -83     51   -509       C  
ATOM   2787  C   PHE B  37     -14.748  46.577  55.842  1.00 26.91           C  
ANISOU 2787  C   PHE B  37     3570   3106   3548    -91     72   -497       C  
ATOM   2788  O   PHE B  37     -15.468  46.355  54.867  1.00 23.10           O  
ANISOU 2788  O   PHE B  37     3078   2611   3086    -84     83   -445       O  
ATOM   2789  CB  PHE B  37     -15.579  45.812  58.071  1.00 24.55           C  
ANISOU 2789  CB  PHE B  37     3302   2872   3155    -63     77   -529       C  
ATOM   2790  CG  PHE B  37     -15.694  44.683  59.047  1.00 21.59           C  
ANISOU 2790  CG  PHE B  37     2943   2550   2711    -48     66   -522       C  
ATOM   2791  CD1 PHE B  37     -14.920  44.657  60.194  1.00 24.32           C  
ANISOU 2791  CD1 PHE B  37     3300   2931   3008    -44     47   -571       C  
ATOM   2792  CD2 PHE B  37     -16.560  43.627  58.790  1.00 25.04           C  
ANISOU 2792  CD2 PHE B  37     3381   3001   3133    -35     75   -466       C  
ATOM   2793  CE1 PHE B  37     -15.036  43.607  61.104  1.00 22.35           C  
ANISOU 2793  CE1 PHE B  37     3068   2732   2692    -23     40   -557       C  
ATOM   2794  CE2 PHE B  37     -16.664  42.567  59.677  1.00 25.51           C  
ANISOU 2794  CE2 PHE B  37     3456   3103   3134    -19     72   -454       C  
ATOM   2795  CZ  PHE B  37     -15.909  42.566  60.838  1.00 25.00           C  
ANISOU 2795  CZ  PHE B  37     3407   3075   3018    -10     56   -497       C  
ATOM   2796  N  ASER B  38     -14.073  47.716  55.977  0.53 25.55           N  
ANISOU 2796  N  ASER B  38     3394   2902   3412   -105     80   -545       N  
ATOM   2797  N  BSER B  38     -14.073  47.723  55.988  0.47 25.54           N  
ANISOU 2797  N  BSER B  38     3394   2901   3411   -105     80   -546       N  
ATOM   2798  CA ASER B  38     -14.204  48.754  54.967  0.53 24.12           C  
ANISOU 2798  CA ASER B  38     3202   2665   3299   -109    107   -530       C  
ATOM   2799  CA BSER B  38     -14.139  48.775  54.979  0.47 24.18           C  
ANISOU 2799  CA BSER B  38     3209   2672   3307   -110    107   -533       C  
ATOM   2800  C  ASER B  38     -13.605  48.313  53.632  0.53 21.56           C  
ANISOU 2800  C  ASER B  38     2863   2334   2995   -119     91   -485       C  
ATOM   2801  C  BSER B  38     -13.624  48.280  53.636  0.47 21.58           C  
ANISOU 2801  C  BSER B  38     2866   2338   2996   -118     91   -484       C  
ATOM   2802  O  ASER B  38     -14.118  48.699  52.573  0.53 24.51           O  
ANISOU 2802  O  ASER B  38     3228   2678   3406   -110    113   -442       O  
ATOM   2803  O  BSER B  38     -14.189  48.610  52.585  0.47 24.49           O  
ANISOU 2803  O  BSER B  38     3226   2679   3400   -108    112   -439       O  
ATOM   2804  CB ASER B  38     -13.566  50.053  55.482  0.53 23.91           C  
ANISOU 2804  CB ASER B  38     3174   2601   3311   -125    124   -597       C  
ATOM   2805  CB BSER B  38     -13.325  49.991  55.436  0.47 24.13           C  
ANISOU 2805  CB BSER B  38     3200   2630   3338   -129    118   -600       C  
ATOM   2806  OG ASER B  38     -13.989  51.144  54.682  0.53 24.71           O  
ANISOU 2806  OG ASER B  38     3268   2642   3479   -121    164   -579       O  
ATOM   2807  OG BSER B  38     -13.876  50.575  56.583  0.47 25.68           O  
ANISOU 2807  OG BSER B  38     3408   2825   3522   -120    138   -647       O  
ATOM   2808  N   MET B  39     -12.543  47.493  53.649  1.00 21.78           N  
ANISOU 2808  N   MET B  39     2887   2392   2995   -134     55   -492       N  
ATOM   2809  CA  MET B  39     -12.016  46.958  52.398  1.00 25.76           C  
ANISOU 2809  CA  MET B  39     3380   2894   3513   -141     41   -448       C  
ATOM   2810  C   MET B  39     -13.050  46.072  51.719  1.00 23.00           C  
ANISOU 2810  C   MET B  39     3032   2564   3145   -123     41   -388       C  
ATOM   2811  O   MET B  39     -13.160  46.069  50.497  1.00 22.70           O  
ANISOU 2811  O   MET B  39     2983   2511   3130   -120     47   -346       O  
ATOM   2812  CB  MET B  39     -10.725  46.155  52.623  1.00 21.33           C  
ANISOU 2812  CB  MET B  39     2814   2366   2923   -157      2   -466       C  
ATOM   2813  CG  MET B  39      -9.625  46.998  53.245  1.00 36.98           C  
ANISOU 2813  CG  MET B  39     4789   4335   4927   -178     -3   -532       C  
ATOM   2814  SD  MET B  39      -8.082  46.089  53.320  1.00 50.68           S  
ANISOU 2814  SD  MET B  39     6512   6109   6636   -194    -48   -547       S  
ATOM   2815  CE  MET B  39      -7.765  45.872  51.568  1.00 45.68           C  
ANISOU 2815  CE  MET B  39     5866   5448   6043   -200    -41   -486       C  
ATOM   2816  N   LEU B  40     -13.787  45.285  52.502  1.00 22.88           N  
ANISOU 2816  N   LEU B  40     3026   2583   3084   -111     36   -384       N  
ATOM   2817  CA  LEU B  40     -14.845  44.472  51.911  1.00 24.52           C  
ANISOU 2817  CA  LEU B  40     3230   2807   3280    -97     40   -333       C  
ATOM   2818  C   LEU B  40     -15.924  45.355  51.283  1.00 19.87           C  
ANISOU 2818  C   LEU B  40     2632   2188   2729    -82     71   -310       C  
ATOM   2819  O   LEU B  40     -16.381  45.094  50.169  1.00 23.73           O  
ANISOU 2819  O   LEU B  40     3108   2678   3230    -74     71   -267       O  
ATOM   2820  CB  LEU B  40     -15.462  43.560  52.985  1.00 20.90           C  
ANISOU 2820  CB  LEU B  40     2784   2385   2773    -88     38   -336       C  
ATOM   2821  CG  LEU B  40     -14.599  42.441  53.572  1.00 26.62           C  
ANISOU 2821  CG  LEU B  40     3517   3145   3452    -94     10   -344       C  
ATOM   2822  CD1 LEU B  40     -15.487  41.651  54.560  1.00 28.52           C  
ANISOU 2822  CD1 LEU B  40     3771   3415   3651    -78     21   -337       C  
ATOM   2823  CD2 LEU B  40     -13.975  41.505  52.492  1.00 28.54           C  
ANISOU 2823  CD2 LEU B  40     3752   3396   3698   -105    -13   -311       C  
ATOM   2824  N   ALA B  41     -16.367  46.397  52.004  1.00 19.81           N  
ANISOU 2824  N   ALA B  41     2630   2157   2739    -73     98   -339       N  
ATOM   2825  CA  ALA B  41     -17.357  47.295  51.415  1.00 26.78           C  
ANISOU 2825  CA  ALA B  41     3504   3010   3662    -54    130   -314       C  
ATOM   2826  C   ALA B  41     -16.840  47.941  50.119  1.00 20.50           C  
ANISOU 2826  C   ALA B  41     2698   2182   2910    -55    136   -288       C  
ATOM   2827  O   ALA B  41     -17.584  48.031  49.130  1.00 22.74           O  
ANISOU 2827  O   ALA B  41     2967   2462   3209    -36    146   -242       O  
ATOM   2828  CB  ALA B  41     -17.783  48.353  52.437  1.00 20.49           C  
ANISOU 2828  CB  ALA B  41     2718   2188   2881    -46    162   -354       C  
ATOM   2829  N   ALA B  42     -15.585  48.410  50.105  1.00 20.41           N  
ANISOU 2829  N   ALA B  42     2688   2147   2918    -75    132   -317       N  
ATOM   2830  CA  ALA B  42     -15.041  49.049  48.897  1.00 26.17           C  
ANISOU 2830  CA  ALA B  42     3408   2842   3692    -76    144   -290       C  
ATOM   2831  C   ALA B  42     -15.014  48.076  47.716  1.00 28.68           C  
ANISOU 2831  C   ALA B  42     3717   3190   3990    -72    121   -240       C  
ATOM   2832  O   ALA B  42     -15.356  48.432  46.574  1.00 23.09           O  
ANISOU 2832  O   ALA B  42     3000   2470   3304    -53    135   -195       O  
ATOM   2833  CB  ALA B  42     -13.623  49.575  49.158  1.00 21.51           C  
ANISOU 2833  CB  ALA B  42     2820   2226   3128   -103    142   -335       C  
ATOM   2834  N   TYR B  43     -14.538  46.858  47.965  1.00 22.65           N  
ANISOU 2834  N   TYR B  43     2956   2466   3184    -87     86   -247       N  
ATOM   2835  CA  TYR B  43     -14.535  45.807  46.945  1.00 20.16           C  
ANISOU 2835  CA  TYR B  43     2633   2181   2846    -85     63   -207       C  
ATOM   2836  C   TYR B  43     -15.940  45.520  46.421  1.00 20.53           C  
ANISOU 2836  C   TYR B  43     2670   2248   2884    -62     69   -168       C  
ATOM   2837  O   TYR B  43     -16.143  45.403  45.201  1.00 22.37           O  
ANISOU 2837  O   TYR B  43     2890   2487   3121    -50     67   -129       O  
ATOM   2838  CB  TYR B  43     -13.913  44.548  47.552  1.00 18.77           C  
ANISOU 2838  CB  TYR B  43     2463   2040   2628   -103     31   -225       C  
ATOM   2839  CG  TYR B  43     -13.963  43.301  46.714  1.00 22.30           C  
ANISOU 2839  CG  TYR B  43     2904   2518   3049   -104      9   -192       C  
ATOM   2840  CD1 TYR B  43     -13.009  43.067  45.731  1.00 30.15           C  
ANISOU 2840  CD1 TYR B  43     3894   3511   4051   -113     -3   -177       C  
ATOM   2841  CD2 TYR B  43     -14.903  42.301  46.977  1.00 21.14           C  
ANISOU 2841  CD2 TYR B  43     2757   2403   2873    -98      2   -181       C  
ATOM   2842  CE1 TYR B  43     -13.003  41.883  45.002  1.00 31.69           C  
ANISOU 2842  CE1 TYR B  43     4085   3735   4222   -115    -22   -154       C  
ATOM   2843  CE2 TYR B  43     -14.916  41.130  46.249  1.00 19.96           C  
ANISOU 2843  CE2 TYR B  43     2601   2280   2705   -103    -16   -158       C  
ATOM   2844  CZ  TYR B  43     -13.949  40.920  45.276  1.00 24.17           C  
ANISOU 2844  CZ  TYR B  43     3131   2811   3243   -111    -29   -146       C  
ATOM   2845  OH  TYR B  43     -13.952  39.740  44.571  1.00 25.44           O  
ANISOU 2845  OH  TYR B  43     3286   2996   3383   -116    -45   -129       O  
ATOM   2846  N   MET B  44     -16.924  45.418  47.314  1.00 19.05           N  
ANISOU 2846  N   MET B  44     2484   2070   2683    -53     78   -180       N  
ATOM   2847  CA  MET B  44     -18.279  45.099  46.865  1.00 20.42           C  
ANISOU 2847  CA  MET B  44     2643   2266   2851    -33     82   -147       C  
ATOM   2848  C   MET B  44     -18.862  46.258  46.078  1.00 25.89           C  
ANISOU 2848  C   MET B  44     3324   2934   3580     -6    108   -119       C  
ATOM   2849  O   MET B  44     -19.585  46.051  45.097  1.00 21.69           O  
ANISOU 2849  O   MET B  44     2773   2423   3045     12    104    -81       O  
ATOM   2850  CB  MET B  44     -19.189  44.765  48.055  1.00 21.86           C  
ANISOU 2850  CB  MET B  44     2829   2464   3015    -30     91   -166       C  
ATOM   2851  CG  MET B  44     -18.862  43.430  48.722  1.00 18.87           C  
ANISOU 2851  CG  MET B  44     2459   2115   2595    -48     69   -180       C  
ATOM   2852  SD  MET B  44     -18.697  42.058  47.548  1.00 23.20           S  
ANISOU 2852  SD  MET B  44     2994   2695   3126    -59     40   -149       S  
ATOM   2853  CE  MET B  44     -20.241  42.137  46.569  1.00 20.25           C  
ANISOU 2853  CE  MET B  44     2591   2338   2768    -37     48   -114       C  
ATOM   2854  N   PHE B  45     -18.544  47.489  46.489  1.00 21.81           N  
ANISOU 2854  N   PHE B  45     2817   2373   3097     -3    136   -137       N  
ATOM   2855  CA  PHE B  45     -19.029  48.654  45.760  1.00 24.09           C  
ANISOU 2855  CA  PHE B  45     3096   2631   3425     26    168   -106       C  
ATOM   2856  C   PHE B  45     -18.496  48.642  44.340  1.00 24.38           C  
ANISOU 2856  C   PHE B  45     3125   2670   3468     33    161    -66       C  
ATOM   2857  O   PHE B  45     -19.236  48.899  43.380  1.00 22.30           O  
ANISOU 2857  O   PHE B  45     2847   2417   3210     64    169    -21       O  
ATOM   2858  CB  PHE B  45     -18.599  49.941  46.478  1.00 24.52           C  
ANISOU 2858  CB  PHE B  45     3164   2630   3522     23    203   -139       C  
ATOM   2859  CG  PHE B  45     -19.219  51.191  45.916  1.00 25.84           C  
ANISOU 2859  CG  PHE B  45     3325   2758   3734     56    245   -107       C  
ATOM   2860  CD1 PHE B  45     -20.588  51.304  45.812  1.00 24.45           C  
ANISOU 2860  CD1 PHE B  45     3135   2599   3557     89    258    -78       C  
ATOM   2861  CD2 PHE B  45     -18.436  52.269  45.565  1.00 25.98           C  
ANISOU 2861  CD2 PHE B  45     3349   2722   3801     56    276   -107       C  
ATOM   2862  CE1 PHE B  45     -21.186  52.469  45.320  1.00 33.70           C  
ANISOU 2862  CE1 PHE B  45     4300   3735   4771    126    298    -45       C  
ATOM   2863  CE2 PHE B  45     -19.006  53.452  45.111  1.00 21.78           C  
ANISOU 2863  CE2 PHE B  45     2813   2148   3315     90    322    -76       C  
ATOM   2864  CZ  PHE B  45     -20.396  53.538  44.977  1.00 30.08           C  
ANISOU 2864  CZ  PHE B  45     3851   3219   4360    127    332    -42       C  
ATOM   2865  N  ALEU B  46     -17.211  48.338  44.181  0.66 24.23           N  
ANISOU 2865  N  ALEU B  46     3115   2645   3446      7    146    -80       N  
ATOM   2866  N  BLEU B  46     -17.210  48.339  44.185  0.34 24.21           N  
ANISOU 2866  N  BLEU B  46     3113   2642   3444      7    146    -80       N  
ATOM   2867  CA ALEU B  46     -16.638  48.265  42.845  0.66 22.17           C  
ANISOU 2867  CA ALEU B  46     2848   2387   3187     14    140    -43       C  
ATOM   2868  CA BLEU B  46     -16.627  48.257  42.855  0.34 22.25           C  
ANISOU 2868  CA BLEU B  46     2859   2398   3198     14    140    -43       C  
ATOM   2869  C  ALEU B  46     -17.319  47.189  42.013  0.66 26.43           C  
ANISOU 2869  C  ALEU B  46     3374   2983   3687     26    111    -12       C  
ATOM   2870  C  BLEU B  46     -17.319  47.190  42.020  0.34 26.33           C  
ANISOU 2870  C  BLEU B  46     3361   2970   3674     26    111    -12       C  
ATOM   2871  O  ALEU B  46     -17.621  47.406  40.829  0.66 22.19           O  
ANISOU 2871  O  ALEU B  46     2825   2457   3149     52    116     32       O  
ATOM   2872  O  BLEU B  46     -17.629  47.416  40.841  0.34 22.33           O  
ANISOU 2872  O  BLEU B  46     2843   2474   3167     53    116     32       O  
ATOM   2873  CB ALEU B  46     -15.133  48.002  42.929  0.66 24.39           C  
ANISOU 2873  CB ALEU B  46     3139   2656   3471    -18    128    -69       C  
ATOM   2874  CB BLEU B  46     -15.126  47.978  42.971  0.34 24.38           C  
ANISOU 2874  CB BLEU B  46     3139   2656   3470    -19    127    -70       C  
ATOM   2875  CG ALEU B  46     -14.400  48.006  41.580  0.66 29.19           C  
ANISOU 2875  CG ALEU B  46     3744   3262   4086    -12    129    -32       C  
ATOM   2876  CG BLEU B  46     -14.242  47.982  41.717  0.34 29.12           C  
ANISOU 2876  CG BLEU B  46     3736   3251   4078    -18    127    -39       C  
ATOM   2877  CD1ALEU B  46     -14.233  49.434  41.026  0.66 29.71           C  
ANISOU 2877  CD1ALEU B  46     3810   3275   4204      8    175     -6       C  
ATOM   2878  CD1BLEU B  46     -14.302  46.652  40.975  0.34 31.35           C  
ANISOU 2878  CD1BLEU B  46     4012   3586   4313    -19     91    -19       C  
ATOM   2879  CD2ALEU B  46     -13.051  47.300  41.688  0.66 28.71           C  
ANISOU 2879  CD2ALEU B  46     3687   3206   4014    -46    105    -57       C  
ATOM   2880  CD2BLEU B  46     -14.589  49.146  40.788  0.34 29.46           C  
ANISOU 2880  CD2BLEU B  46     3775   3263   4157     16    167      6       C  
ATOM   2881  N   LEU B  47     -17.568  46.018  42.611  1.00 21.38           N  
ANISOU 2881  N   LEU B  47     2732   2378   3012      7     83    -34       N  
ATOM   2882  CA  LEU B  47     -18.171  44.924  41.847  1.00 23.38           C  
ANISOU 2882  CA  LEU B  47     2970   2681   3232     12     56    -13       C  
ATOM   2883  C   LEU B  47     -19.575  45.286  41.368  1.00 27.18           C  
ANISOU 2883  C   LEU B  47     3429   3182   3715     46     66     17       C  
ATOM   2884  O   LEU B  47     -19.982  44.902  40.265  1.00 23.60           O  
ANISOU 2884  O   LEU B  47     2959   2765   3245     62     50     45       O  
ATOM   2885  CB  LEU B  47     -18.209  43.654  42.691  1.00 22.74           C  
ANISOU 2885  CB  LEU B  47     2893   2625   3121    -15     33    -43       C  
ATOM   2886  CG  LEU B  47     -16.881  42.967  43.008  1.00 20.72           C  
ANISOU 2886  CG  LEU B  47     2653   2366   2853    -44     16    -66       C  
ATOM   2887  CD1 LEU B  47     -17.237  41.642  43.740  1.00 21.02           C  
ANISOU 2887  CD1 LEU B  47     2693   2433   2861    -61     -1    -84       C  
ATOM   2888  CD2 LEU B  47     -16.250  42.683  41.631  1.00 28.87           C  
ANISOU 2888  CD2 LEU B  47     3681   3410   3880    -42      4    -41       C  
ATOM   2889  N   ILE B  48     -20.351  45.963  42.213  1.00 21.95           N  
ANISOU 2889  N   ILE B  48     2767   2502   3073     58     89      8       N  
ATOM   2890  CA  ILE B  48     -21.669  46.439  41.804  1.00 20.26           C  
ANISOU 2890  CA  ILE B  48     2528   2303   2866     94    101     37       C  
ATOM   2891  C   ILE B  48     -21.539  47.489  40.703  1.00 23.64           C  
ANISOU 2891  C   ILE B  48     2953   2715   3315    129    120     81       C  
ATOM   2892  O   ILE B  48     -22.232  47.426  39.683  1.00 23.38           O  
ANISOU 2892  O   ILE B  48     2897   2719   3268    159    111    117       O  
ATOM   2893  CB  ILE B  48     -22.430  46.990  43.021  1.00 23.96           C  
ANISOU 2893  CB  ILE B  48     2999   2749   3353     99    127     17       C  
ATOM   2894  CG1 ILE B  48     -22.821  45.841  43.967  1.00 20.84           C  
ANISOU 2894  CG1 ILE B  48     2604   2381   2933     74    110    -14       C  
ATOM   2895  CG2 ILE B  48     -23.630  47.856  42.596  1.00 28.42           C  
ANISOU 2895  CG2 ILE B  48     3543   3318   3940    143    150     52       C  
ATOM   2896  CD1 ILE B  48     -23.109  46.372  45.418  1.00 24.52           C  
ANISOU 2896  CD1 ILE B  48     3086   2819   3413     71    138    -46       C  
ATOM   2897  N   MET B  49     -20.648  48.481  40.896  1.00 24.05           N  
ANISOU 2897  N   MET B  49     3026   2712   3400    126    149     77       N  
ATOM   2898  CA  MET B  49     -20.577  49.571  39.918  1.00 24.12           C  
ANISOU 2898  CA  MET B  49     3033   2697   3436    164    179    124       C  
ATOM   2899  C   MET B  49     -20.013  49.107  38.587  1.00 32.03           C  
ANISOU 2899  C   MET B  49     4030   3728   4411    171    159    156       C  
ATOM   2900  O   MET B  49     -20.325  49.704  37.549  1.00 28.65           O  
ANISOU 2900  O   MET B  49     3592   3308   3986    212    174    206       O  
ATOM   2901  CB  MET B  49     -19.747  50.745  40.460  1.00 28.94           C  
ANISOU 2901  CB  MET B  49     3664   3235   4096    155    220    108       C  
ATOM   2902  CG  MET B  49     -20.388  51.386  41.673  1.00 25.38           C  
ANISOU 2902  CG  MET B  49     3217   2753   3672    156    246     78       C  
ATOM   2903  SD  MET B  49     -21.975  52.178  41.323  1.00 41.34           S  
ANISOU 2903  SD  MET B  49     5218   4781   5710    214    275    125       S  
ATOM   2904  CE  MET B  49     -21.455  53.344  40.076  1.00 43.10           C  
ANISOU 2904  CE  MET B  49     5444   4963   5969    252    314    183       C  
ATOM   2905  N   LEU B  50     -19.157  48.083  38.583  1.00 27.35           N  
ANISOU 2905  N   LEU B  50     3446   3154   3794    134    128    131       N  
ATOM   2906  CA  LEU B  50     -18.760  47.496  37.300  1.00 23.80           C  
ANISOU 2906  CA  LEU B  50     2990   2741   3313    142    107    158       C  
ATOM   2907  C   LEU B  50     -19.767  46.453  36.825  1.00 28.79           C  
ANISOU 2907  C   LEU B  50     3597   3441   3901    150     70    162       C  
ATOM   2908  O   LEU B  50     -20.037  46.347  35.621  1.00 25.32           O  
ANISOU 2908  O   LEU B  50     3144   3042   3436    179     59    197       O  
ATOM   2909  CB  LEU B  50     -17.392  46.817  37.396  1.00 28.80           C  
ANISOU 2909  CB  LEU B  50     3641   3365   3939    102     92    131       C  
ATOM   2910  CG  LEU B  50     -16.177  47.719  37.636  1.00 45.02           C  
ANISOU 2910  CG  LEU B  50     5713   5356   6035     89    124    125       C  
ATOM   2911  CD1 LEU B  50     -14.888  46.905  37.540  1.00 45.16           C  
ANISOU 2911  CD1 LEU B  50     5740   5377   6040     54    103    103       C  
ATOM   2912  CD2 LEU B  50     -16.151  48.898  36.666  1.00 49.70           C  
ANISOU 2912  CD2 LEU B  50     6305   5922   6655    129    163    177       C  
ATOM   2913  N   GLY B  51     -20.297  45.668  37.765  1.00 25.59           N  
ANISOU 2913  N   GLY B  51     3186   3051   3486    125     52    125       N  
ATOM   2914  CA  GLY B  51     -21.160  44.541  37.403  1.00 21.92           C  
ANISOU 2914  CA  GLY B  51     2697   2646   2987    122     19    119       C  
ATOM   2915  C   GLY B  51     -22.462  44.951  36.733  1.00 28.50           C  
ANISOU 2915  C   GLY B  51     3498   3517   3814    166     18    150       C  
ATOM   2916  O   GLY B  51     -22.909  44.302  35.783  1.00 26.84           O  
ANISOU 2916  O   GLY B  51     3265   3363   3572    176    -10    159       O  
ATOM   2917  N   PHE B  52     -23.113  46.010  37.227  1.00 21.87           N  
ANISOU 2917  N   PHE B  52     2654   2650   3004    192     48    165       N  
ATOM   2918  CA  PHE B  52     -24.379  46.394  36.601  1.00 27.31           C  
ANISOU 2918  CA  PHE B  52     3310   3380   3688    238     47    198       C  
ATOM   2919  C   PHE B  52     -24.202  46.834  35.145  1.00 29.02           C  
ANISOU 2919  C   PHE B  52     3520   3623   3885    280     44    246       C  
ATOM   2920  O   PHE B  52     -24.845  46.238  34.262  1.00 29.32           O  
ANISOU 2920  O   PHE B  52     3528   3727   3886    297     12    255       O  
ATOM   2921  CB  PHE B  52     -25.100  47.445  37.461  1.00 26.80           C  
ANISOU 2921  CB  PHE B  52     3244   3278   3662    259     84    204       C  
ATOM   2922  CG  PHE B  52     -26.162  48.215  36.712  1.00 33.21           C  
ANISOU 2922  CG  PHE B  52     4026   4118   4476    319     94    251       C  
ATOM   2923  CD1 PHE B  52     -27.256  47.561  36.156  1.00 34.67           C  
ANISOU 2923  CD1 PHE B  52     4168   4373   4632    335     61    255       C  
ATOM   2924  CD2 PHE B  52     -26.066  49.588  36.561  1.00 46.18           C  
ANISOU 2924  CD2 PHE B  52     5681   5715   6151    359    137    291       C  
ATOM   2925  CE1 PHE B  52     -28.237  48.268  35.478  1.00 39.10           C  
ANISOU 2925  CE1 PHE B  52     4697   4966   5192    394     67    300       C  
ATOM   2926  CE2 PHE B  52     -27.039  50.303  35.864  1.00 51.03           C  
ANISOU 2926  CE2 PHE B  52     6267   6356   6767    420    148    340       C  
ATOM   2927  CZ  PHE B  52     -28.123  49.639  35.325  1.00 50.09           C  
ANISOU 2927  CZ  PHE B  52     6104   6314   6614    438    111    345       C  
ATOM   2928  N   PRO B  53     -23.329  47.793  34.811  1.00 28.15           N  
ANISOU 2928  N   PRO B  53     3434   3467   3794    297     76    277       N  
ATOM   2929  CA  PRO B  53     -23.240  48.228  33.406  1.00 27.28           C  
ANISOU 2929  CA  PRO B  53     3318   3385   3662    345     79    331       C  
ATOM   2930  C   PRO B  53     -22.720  47.163  32.455  1.00 23.11           C  
ANISOU 2930  C   PRO B  53     2788   2910   3085    331     40    324       C  
ATOM   2931  O   PRO B  53     -23.246  47.051  31.341  1.00 25.62           O  
ANISOU 2931  O   PRO B  53     3082   3288   3364    370     21    354       O  
ATOM   2932  CB  PRO B  53     -22.291  49.440  33.450  1.00 34.97           C  
ANISOU 2932  CB  PRO B  53     4323   4285   4678    356    130    359       C  
ATOM   2933  CG  PRO B  53     -22.190  49.824  34.885  1.00 46.34           C  
ANISOU 2933  CG  PRO B  53     5779   5663   6166    324    154    320       C  
ATOM   2934  CD  PRO B  53     -22.481  48.602  35.701  1.00 29.12           C  
ANISOU 2934  CD  PRO B  53     3590   3512   3964    278    115    264       C  
ATOM   2935  N   ILE B  54     -21.678  46.408  32.826  1.00 21.48           N  
ANISOU 2935  N   ILE B  54     2603   2681   2877    280     30    286       N  
ATOM   2936  CA  ILE B  54     -21.152  45.445  31.876  1.00 24.74           C  
ANISOU 2936  CA  ILE B  54     3015   3140   3246    269     -2    280       C  
ATOM   2937  C   ILE B  54     -22.190  44.368  31.574  1.00 27.73           C  
ANISOU 2937  C   ILE B  54     3359   3592   3587    266    -46    256       C  
ATOM   2938  O   ILE B  54     -22.307  43.917  30.428  1.00 27.21           O  
ANISOU 2938  O   ILE B  54     3277   3584   3476    285    -71    267       O  
ATOM   2939  CB  ILE B  54     -19.816  44.838  32.355  1.00 30.62           C  
ANISOU 2939  CB  ILE B  54     3789   3846   4001    217     -3    246       C  
ATOM   2940  CG1 ILE B  54     -19.159  44.133  31.162  1.00 44.15           C  
ANISOU 2940  CG1 ILE B  54     5504   5598   5672    219    -23    253       C  
ATOM   2941  CG2 ILE B  54     -20.012  43.839  33.476  1.00 39.67           C  
ANISOU 2941  CG2 ILE B  54     4932   4990   5150    169    -24    191       C  
ATOM   2942  CD1 ILE B  54     -17.642  43.979  31.249  1.00 49.12           C  
ANISOU 2942  CD1 ILE B  54     6163   6185   6314    188    -11    243       C  
ATOM   2943  N   ASN B  55     -22.963  43.947  32.580  1.00 23.57           N  
ANISOU 2943  N   ASN B  55     2816   3063   3075    241    -54    221       N  
ATOM   2944  CA  ASN B  55     -23.972  42.923  32.305  1.00 23.12           C  
ANISOU 2944  CA  ASN B  55     2722   3071   2990    234    -92    194       C  
ATOM   2945  C   ASN B  55     -25.186  43.499  31.600  1.00 27.01           C  
ANISOU 2945  C   ASN B  55     3176   3617   3468    288   -100    226       C  
ATOM   2946  O   ASN B  55     -25.748  42.847  30.709  1.00 24.20           O  
ANISOU 2946  O   ASN B  55     2789   3333   3074    299   -135    218       O  
ATOM   2947  CB  ASN B  55     -24.377  42.210  33.588  1.00 20.78           C  
ANISOU 2947  CB  ASN B  55     2421   2756   2717    189    -94    148       C  
ATOM   2948  CG  ASN B  55     -23.321  41.272  34.049  1.00 26.04           C  
ANISOU 2948  CG  ASN B  55     3116   3395   3383    139   -100    113       C  
ATOM   2949  OD1 ASN B  55     -23.119  40.222  33.450  1.00 20.76           O  
ANISOU 2949  OD1 ASN B  55     2439   2760   2687    119   -126     91       O  
ATOM   2950  ND2 ASN B  55     -22.622  41.637  35.119  1.00 23.98           N  
ANISOU 2950  ND2 ASN B  55     2886   3074   3151    118    -75    105       N  
ATOM   2951  N   PHE B  56     -25.603  44.716  31.973  1.00 21.41           N  
ANISOU 2951  N   PHE B  56     2468   2876   2789    324    -67    262       N  
ATOM   2952  CA  PHE B  56     -26.726  45.339  31.263  1.00 26.40           C  
ANISOU 2952  CA  PHE B  56     3063   3560   3407    384    -71    300       C  
ATOM   2953  C   PHE B  56     -26.379  45.570  29.802  1.00 29.33           C  
ANISOU 2953  C   PHE B  56     3434   3977   3734    428    -82    342       C  
ATOM   2954  O   PHE B  56     -27.223  45.380  28.908  1.00 29.90           O  
ANISOU 2954  O   PHE B  56     3466   4127   3767    465   -112    354       O  
ATOM   2955  CB  PHE B  56     -27.099  46.667  31.910  1.00 30.20           C  
ANISOU 2955  CB  PHE B  56     3551   3989   3933    417    -26    335       C  
ATOM   2956  CG  PHE B  56     -28.262  47.362  31.219  1.00 29.92           C  
ANISOU 2956  CG  PHE B  56     3476   4005   3886    485    -28    380       C  
ATOM   2957  CD1 PHE B  56     -29.563  46.978  31.489  1.00 41.99           C  
ANISOU 2957  CD1 PHE B  56     4959   5582   5414    489    -50    360       C  
ATOM   2958  CD2 PHE B  56     -28.040  48.354  30.289  1.00 38.89           C  
ANISOU 2958  CD2 PHE B  56     4621   5144   5012    546     -6    444       C  
ATOM   2959  CE1 PHE B  56     -30.632  47.592  30.851  1.00 39.76           C  
ANISOU 2959  CE1 PHE B  56     4635   5351   5119    554    -54    401       C  
ATOM   2960  CE2 PHE B  56     -29.106  48.976  29.637  1.00 38.96           C  
ANISOU 2960  CE2 PHE B  56     4593   5205   5006    614     -8    491       C  
ATOM   2961  CZ  PHE B  56     -30.401  48.593  29.940  1.00 41.88           C  
ANISOU 2961  CZ  PHE B  56     4914   5624   5374    618    -34    467       C  
ATOM   2962  N  ALEU B  57     -25.142  45.998  29.535  0.46 23.83           N  
ANISOU 2962  N  ALEU B  57     2778   3235   3043    428    -56    366       N  
ATOM   2963  N  BLEU B  57     -25.143  46.000  29.537  0.54 23.78           N  
ANISOU 2963  N  BLEU B  57     2771   3228   3036    428    -56    366       N  
ATOM   2964  CA ALEU B  57     -24.726  46.238  28.158  0.46 27.70           C  
ANISOU 2964  CA ALEU B  57     3272   3764   3490    472    -59    410       C  
ATOM   2965  CA BLEU B  57     -24.729  46.238  28.161  0.54 27.71           C  
ANISOU 2965  CA BLEU B  57     3273   3765   3491    472    -59    410       C  
ATOM   2966  C  ALEU B  57     -24.707  44.942  27.359  0.46 27.84           C  
ANISOU 2966  C  ALEU B  57     3272   3856   3452    453   -110    374       C  
ATOM   2967  C  BLEU B  57     -24.708  44.943  27.361  0.54 27.85           C  
ANISOU 2967  C  BLEU B  57     3273   3856   3452    453   -110    374       C  
ATOM   2968  O  ALEU B  57     -25.082  44.931  26.183  0.46 25.28           O  
ANISOU 2968  O  ALEU B  57     2927   3604   3076    499   -132    399       O  
ATOM   2969  O  BLEU B  57     -25.081  44.933  26.184  0.54 25.26           O  
ANISOU 2969  O  BLEU B  57     2924   3601   3074    498   -132    399       O  
ATOM   2970  CB ALEU B  57     -23.356  46.907  28.125  0.46 27.57           C  
ANISOU 2970  CB ALEU B  57     3302   3676   3498    468    -16    438       C  
ATOM   2971  CB BLEU B  57     -23.364  46.917  28.125  0.54 27.57           C  
ANISOU 2971  CB BLEU B  57     3301   3675   3497    469    -16    438       C  
ATOM   2972  CG ALEU B  57     -22.814  47.340  26.759  0.46 29.83           C  
ANISOU 2972  CG ALEU B  57     3598   3988   3746    519     -4    494       C  
ATOM   2973  CG BLEU B  57     -23.373  48.435  28.342  0.54 25.70           C  
ANISOU 2973  CG BLEU B  57     3080   3378   3306    512     40    494       C  
ATOM   2974  CD1ALEU B  57     -23.755  48.310  26.067  0.46 30.65           C  
ANISOU 2974  CD1ALEU B  57     3680   4129   3835    598      9    558       C  
ATOM   2975  CD1BLEU B  57     -21.960  48.979  28.309  0.54 29.41           C  
ANISOU 2975  CD1BLEU B  57     3591   3776   3805    499     83    512       C  
ATOM   2976  CD2ALEU B  57     -21.439  47.959  26.934  0.46 32.01           C  
ANISOU 2976  CD2ALEU B  57     3918   4182   4062    503     43    513       C  
ATOM   2977  CD2BLEU B  57     -24.224  49.132  27.298  0.54 33.19           C  
ANISOU 2977  CD2BLEU B  57     4004   4382   4224    592     44    557       C  
ATOM   2978  N   THR B  58     -24.257  43.846  27.976  1.00 23.88           N  
ANISOU 2978  N   THR B  58     2780   3337   2958    387   -127    314       N  
ATOM   2979  CA  THR B  58     -24.295  42.560  27.294  1.00 29.22           C  
ANISOU 2979  CA  THR B  58     3438   4077   3588    364   -172    273       C  
ATOM   2980  C   THR B  58     -25.732  42.184  26.945  1.00 28.07           C  
ANISOU 2980  C   THR B  58     3238   4012   3418    383   -210    255       C  
ATOM   2981  O   THR B  58     -26.016  41.756  25.821  1.00 24.49           O  
ANISOU 2981  O   THR B  58     2760   3636   2911    407   -244    252       O  
ATOM   2982  CB  THR B  58     -23.644  41.495  28.177  1.00 28.27           C  
ANISOU 2982  CB  THR B  58     3337   3915   3491    292   -177    215       C  
ATOM   2983  OG1 THR B  58     -22.264  41.837  28.365  1.00 27.64           O  
ANISOU 2983  OG1 THR B  58     3302   3771   3428    278   -147    231       O  
ATOM   2984  CG2 THR B  58     -23.741  40.113  27.541  1.00 31.29           C  
ANISOU 2984  CG2 THR B  58     3698   4356   3833    264   -219    167       C  
ATOM   2985  N   LEU B  59     -26.654  42.373  27.892  1.00 24.92           N  
ANISOU 2985  N   LEU B  59     2816   3597   3056    376   -204    244       N  
ATOM   2986  CA  LEU B  59     -28.059  42.066  27.638  1.00 27.02           C  
ANISOU 2986  CA  LEU B  59     3025   3937   3307    393   -237    226       C  
ATOM   2987  C   LEU B  59     -28.604  42.917  26.499  1.00 30.70           C  
ANISOU 2987  C   LEU B  59     3466   4467   3732    471   -246    281       C  
ATOM   2988  O   LEU B  59     -29.211  42.402  25.546  1.00 28.62           O  
ANISOU 2988  O   LEU B  59     3162   4293   3419    491   -288    266       O  
ATOM   2989  CB  LEU B  59     -28.852  42.288  28.936  1.00 25.52           C  
ANISOU 2989  CB  LEU B  59     2821   3707   3170    376   -218    213       C  
ATOM   2990  CG  LEU B  59     -30.364  42.052  29.032  1.00 35.89           C  
ANISOU 2990  CG  LEU B  59     4072   5078   4487    386   -242    193       C  
ATOM   2991  CD1 LEU B  59     -30.737  41.871  30.515  1.00 34.61           C  
ANISOU 2991  CD1 LEU B  59     3912   4858   4381    343   -217    163       C  
ATOM   2992  CD2 LEU B  59     -31.132  43.236  28.479  1.00 48.43           C  
ANISOU 2992  CD2 LEU B  59     5634   6702   6065    463   -236    251       C  
ATOM   2993  N   TYR B  60     -28.347  44.225  26.568  1.00 27.33           N  
ANISOU 2993  N   TYR B  60     3064   3996   3325    518   -203    345       N  
ATOM   2994  CA  TYR B  60     -28.885  45.181  25.607  1.00 27.40           C  
ANISOU 2994  CA  TYR B  60     3053   4056   3301    600   -201    410       C  
ATOM   2995  C   TYR B  60     -28.398  44.891  24.189  1.00 25.12           C  
ANISOU 2995  C   TYR B  60     2767   3834   2942    631   -226    426       C  
ATOM   2996  O   TYR B  60     -29.199  44.802  23.241  1.00 30.82           O  
ANISOU 2996  O   TYR B  60     3446   4652   3612    678   -262    435       O  
ATOM   2997  CB  TYR B  60     -28.465  46.588  26.039  1.00 27.59           C  
ANISOU 2997  CB  TYR B  60     3114   3999   3370    634   -140    473       C  
ATOM   2998  CG  TYR B  60     -29.150  47.660  25.207  1.00 30.15           C  
ANISOU 2998  CG  TYR B  60     3416   4367   3672    725   -128    546       C  
ATOM   2999  CD1 TYR B  60     -30.357  48.181  25.599  1.00 38.09           C  
ANISOU 2999  CD1 TYR B  60     4384   5388   4699    759   -126    561       C  
ATOM   3000  CD2 TYR B  60     -28.567  48.128  24.047  1.00 39.05           C  
ANISOU 3000  CD2 TYR B  60     4563   5520   4756    778   -118    603       C  
ATOM   3001  CE1 TYR B  60     -30.991  49.156  24.839  1.00 52.50           C  
ANISOU 3001  CE1 TYR B  60     6189   7256   6504    847   -114    632       C  
ATOM   3002  CE2 TYR B  60     -29.174  49.097  23.278  1.00 41.43           C  
ANISOU 3002  CE2 TYR B  60     4846   5862   5034    867   -105    676       C  
ATOM   3003  CZ  TYR B  60     -30.390  49.604  23.678  1.00 46.92           C  
ANISOU 3003  CZ  TYR B  60     5501   6574   5751    902   -104    691       C  
ATOM   3004  OH  TYR B  60     -30.995  50.570  22.910  1.00 52.05           O  
ANISOU 3004  OH  TYR B  60     6133   7268   6377    995    -90    768       O  
ATOM   3005  N   VAL B  61     -27.083  44.734  24.037  1.00 26.30           N  
ANISOU 3005  N   VAL B  61     2965   3938   3091    605   -207    428       N  
ATOM   3006  CA  VAL B  61     -26.494  44.464  22.734  1.00 32.00           C  
ANISOU 3006  CA  VAL B  61     3696   4716   3748    632   -224    444       C  
ATOM   3007  C   VAL B  61     -27.061  43.177  22.150  1.00 31.47           C  
ANISOU 3007  C   VAL B  61     3587   4741   3628    610   -286    379       C  
ATOM   3008  O   VAL B  61     -27.405  43.112  20.963  1.00 37.88           O  
ANISOU 3008  O   VAL B  61     4375   5644   4373    659   -316    393       O  
ATOM   3009  CB  VAL B  61     -24.962  44.385  22.848  1.00 29.57           C  
ANISOU 3009  CB  VAL B  61     3445   4335   3457    596   -191    446       C  
ATOM   3010  CG1 VAL B  61     -24.362  43.834  21.546  1.00 29.66           C  
ANISOU 3010  CG1 VAL B  61     3463   4408   3398    613   -213    447       C  
ATOM   3011  CG2 VAL B  61     -24.366  45.753  23.201  1.00 37.93           C  
ANISOU 3011  CG2 VAL B  61     4540   5308   4562    625   -128    512       C  
ATOM   3012  N   THR B  62     -27.148  42.127  22.966  1.00 30.57           N  
ANISOU 3012  N   THR B  62     3464   4605   3544    536   -304    306       N  
ATOM   3013  CA  THR B  62     -27.674  40.862  22.467  1.00 30.77           C  
ANISOU 3013  CA  THR B  62     3450   4709   3532    508   -358    238       C  
ATOM   3014  C   THR B  62     -29.102  41.026  21.970  1.00 33.60           C  
ANISOU 3014  C   THR B  62     3744   5162   3861    555   -395    238       C  
ATOM   3015  O   THR B  62     -29.451  40.556  20.884  1.00 32.91           O  
ANISOU 3015  O   THR B  62     3625   5170   3710    578   -438    218       O  
ATOM   3016  CB  THR B  62     -27.610  39.795  23.556  1.00 29.78           C  
ANISOU 3016  CB  THR B  62     3326   4534   3456    424   -361    167       C  
ATOM   3017  OG1 THR B  62     -26.250  39.654  24.004  1.00 26.95           O  
ANISOU 3017  OG1 THR B  62     3025   4094   3122    386   -329    168       O  
ATOM   3018  CG2 THR B  62     -28.091  38.456  22.965  1.00 34.46           C  
ANISOU 3018  CG2 THR B  62     3877   5202   4013    392   -412     93       C  
ATOM   3019  N   VAL B  63     -29.943  41.700  22.752  1.00 28.17           N  
ANISOU 3019  N   VAL B  63     3035   4451   3217    570   -379    259       N  
ATOM   3020  CA  VAL B  63     -31.345  41.851  22.352  1.00 38.60           C  
ANISOU 3020  CA  VAL B  63     4289   5861   4515    614   -414    259       C  
ATOM   3021  C   VAL B  63     -31.479  42.724  21.103  1.00 40.71           C  
ANISOU 3021  C   VAL B  63     4549   6202   4718    706   -422    327       C  
ATOM   3022  O   VAL B  63     -32.359  42.484  20.262  1.00 39.83           O  
ANISOU 3022  O   VAL B  63     4381   6198   4553    744   -470    313       O  
ATOM   3023  CB  VAL B  63     -32.179  42.388  23.535  1.00 36.54           C  
ANISOU 3023  CB  VAL B  63     4009   5553   4321    609   -390    267       C  
ATOM   3024  CG1 VAL B  63     -33.582  42.734  23.113  1.00 41.31           C  
ANISOU 3024  CG1 VAL B  63     4545   6246   4906    665   -420    279       C  
ATOM   3025  CG2 VAL B  63     -32.236  41.331  24.640  1.00 39.97           C  
ANISOU 3025  CG2 VAL B  63     4441   5938   4807    521   -391    193       C  
ATOM   3026  N  AGLN B  64     -30.614  43.731  20.948  0.57 40.14           N  
ANISOU 3026  N  AGLN B  64     4529   6074   4648    746   -374    402       N  
ATOM   3027  N  BGLN B  64     -30.615  43.727  20.951  0.43 40.13           N  
ANISOU 3027  N  BGLN B  64     4527   6073   4646    746   -374    401       N  
ATOM   3028  CA AGLN B  64     -30.719  44.713  19.873  0.57 38.99           C  
ANISOU 3028  CA AGLN B  64     4382   5984   4449    842   -367    482       C  
ATOM   3029  CA BGLN B  64     -30.714  44.714  19.882  0.43 39.05           C  
ANISOU 3029  CA BGLN B  64     4389   5990   4456    841   -367    482       C  
ATOM   3030  C  AGLN B  64     -30.137  44.224  18.548  0.57 47.22           C  
ANISOU 3030  C  AGLN B  64     5433   7101   5408    864   -395    479       C  
ATOM   3031  C  BGLN B  64     -30.130  44.228  18.555  0.43 47.16           C  
ANISOU 3031  C  BGLN B  64     5426   7092   5401    864   -395    480       C  
ATOM   3032  O  AGLN B  64     -30.214  44.950  17.552  0.57 53.44           O  
ANISOU 3032  O  AGLN B  64     6219   7945   6139    947   -392    546       O  
ATOM   3033  O  BGLN B  64     -30.203  44.959  17.561  0.43 53.25           O  
ANISOU 3033  O  BGLN B  64     6196   7921   6117    947   -391    547       O  
ATOM   3034  CB AGLN B  64     -30.017  46.017  20.289  0.57 45.22           C  
ANISOU 3034  CB AGLN B  64     5225   6673   5285    873   -295    563       C  
ATOM   3035  CB BGLN B  64     -30.016  46.009  20.328  0.43 45.22           C  
ANISOU 3035  CB BGLN B  64     5225   6671   5287    871   -294    562       C  
ATOM   3036  CG AGLN B  64     -30.519  47.276  19.590  0.57 49.12           C  
ANISOU 3036  CG AGLN B  64     5707   7203   5752    977   -274    656       C  
ATOM   3037  CG BGLN B  64     -30.407  47.277  19.578  0.43 49.06           C  
ANISOU 3037  CG BGLN B  64     5705   7191   5745    975   -271    657       C  
ATOM   3038  CD AGLN B  64     -29.489  48.399  19.575  0.57 50.09           C  
ANISOU 3038  CD AGLN B  64     5892   7237   5904   1008   -201    735       C  
ATOM   3039  CD BGLN B  64     -31.744  47.860  20.021  0.43 46.05           C  
ANISOU 3039  CD BGLN B  64     5275   6833   5391   1014   -274    676       C  
ATOM   3040  OE1AGLN B  64     -28.303  48.172  19.801  0.57 49.35           O  
ANISOU 3040  OE1AGLN B  64     5846   7072   5831    959   -175    721       O  
ATOM   3041  OE1BGLN B  64     -32.559  47.185  20.651  0.43 50.33           O  
ANISOU 3041  OE1BGLN B  64     5774   7395   5955    969   -308    611       O  
ATOM   3042  NE2AGLN B  64     -29.944  49.619  19.304  0.57 52.36           N  
ANISOU 3042  NE2AGLN B  64     6174   7524   6195   1092   -166    820       N  
ATOM   3043  NE2BGLN B  64     -31.969  49.125  19.692  0.43 49.81           N  
ANISOU 3043  NE2BGLN B  64     5756   7302   5867   1099   -235    766       N  
ATOM   3044  N   HIS B  65     -29.581  43.013  18.495  1.00 39.90           N  
ANISOU 3044  N   HIS B  65     4515   6177   4469    796   -421    406       N  
ATOM   3045  CA  HIS B  65     -28.901  42.524  17.293  1.00 41.36           C  
ANISOU 3045  CA  HIS B  65     4714   6422   4577    812   -442    399       C  
ATOM   3046  C   HIS B  65     -29.360  41.099  16.994  1.00 38.19           C  
ANISOU 3046  C   HIS B  65     4270   6096   4144    761   -504    299       C  
ATOM   3047  O   HIS B  65     -28.803  40.136  17.534  1.00 39.34           O  
ANISOU 3047  O   HIS B  65     4433   6190   4323    681   -504    235       O  
ATOM   3048  CB  HIS B  65     -27.383  42.577  17.453  1.00 44.70           C  
ANISOU 3048  CB  HIS B  65     5209   6753   5024    780   -394    418       C  
ATOM   3049  CG  HIS B  65     -26.820  43.964  17.533  1.00 50.00           C  
ANISOU 3049  CG  HIS B  65     5922   7355   5720    832   -330    515       C  
ATOM   3050  ND1 HIS B  65     -26.309  44.625  16.436  1.00 59.37           N  
ANISOU 3050  ND1 HIS B  65     7133   8574   6852    904   -308    586       N  
ATOM   3051  CD2 HIS B  65     -26.662  44.805  18.585  1.00 44.81           C  
ANISOU 3051  CD2 HIS B  65     5288   6596   5141    822   -280    549       C  
ATOM   3052  CE1 HIS B  65     -25.874  45.817  16.805  1.00 60.33           C  
ANISOU 3052  CE1 HIS B  65     7289   8612   7022    934   -245    662       C  
ATOM   3053  NE2 HIS B  65     -26.080  45.954  18.104  1.00 49.04           N  
ANISOU 3053  NE2 HIS B  65     5859   7101   5674    884   -228    638       N  
ATOM   3054  N   LYS B  66     -30.317  40.969  16.073  1.00 40.57           N  
ANISOU 3054  N   LYS B  66     4515   6520   4378    810   -556    286       N  
ATOM   3055  CA  LYS B  66     -30.893  39.661  15.761  1.00 46.87           C  
ANISOU 3055  CA  LYS B  66     5262   7396   5150    763   -617    185       C  
ATOM   3056  C   LYS B  66     -29.880  38.688  15.162  1.00 40.61           C  
ANISOU 3056  C   LYS B  66     4502   6608   4319    723   -626    136       C  
ATOM   3057  O   LYS B  66     -30.133  37.480  15.152  1.00 47.41           O  
ANISOU 3057  O   LYS B  66     5334   7500   5181    662   -663     42       O  
ATOM   3058  CB  LYS B  66     -32.086  39.823  14.810  1.00 50.22           C  
ANISOU 3058  CB  LYS B  66     5617   7961   5503    832   -672    184       C  
ATOM   3059  CG  LYS B  66     -33.079  40.912  15.235  1.00 54.53           C  
ANISOU 3059  CG  LYS B  66     6130   8513   6077    890   -661    246       C  
ATOM   3060  CD  LYS B  66     -33.495  40.770  16.702  1.00 62.36           C  
ANISOU 3060  CD  LYS B  66     7112   9412   7170    822   -639    216       C  
ATOM   3061  CE  LYS B  66     -34.047  42.077  17.252  1.00 59.72           C  
ANISOU 3061  CE  LYS B  66     6773   9042   6875    880   -603    298       C  
ATOM   3062  NZ  LYS B  66     -34.485  41.949  18.669  1.00 52.13           N  
ANISOU 3062  NZ  LYS B  66     5802   7997   6007    818   -580    267       N  
ATOM   3063  N   LYS B  67     -28.727  39.165  14.697  1.00 44.39           N  
ANISOU 3063  N   LYS B  67     5042   7053   4772    752   -588    194       N  
ATOM   3064  CA  LYS B  67     -27.692  38.244  14.245  1.00 42.60           C  
ANISOU 3064  CA  LYS B  67     4850   6817   4520    710   -590    148       C  
ATOM   3065  C   LYS B  67     -27.084  37.444  15.391  1.00 44.64           C  
ANISOU 3065  C   LYS B  67     5134   6966   4859    613   -567     94       C  
ATOM   3066  O   LYS B  67     -26.391  36.454  15.139  1.00 45.04           O  
ANISOU 3066  O   LYS B  67     5204   7011   4898    566   -574     38       O  
ATOM   3067  CB  LYS B  67     -26.575  39.005  13.530  1.00 47.48           C  
ANISOU 3067  CB  LYS B  67     5527   7418   5097    765   -548    230       C  
ATOM   3068  CG  LYS B  67     -25.810  39.935  14.454  1.00 44.70           C  
ANISOU 3068  CG  LYS B  67     5226   6938   4820    758   -480    300       C  
ATOM   3069  CD  LYS B  67     -24.834  40.830  13.699  1.00 58.66           C  
ANISOU 3069  CD  LYS B  67     7044   8691   6552    821   -434    388       C  
ATOM   3070  N   LEU B  68     -27.292  37.854  16.640  1.00 38.31           N  
ANISOU 3070  N   LEU B  68     4337   6079   4138    585   -538    111       N  
ATOM   3071  CA  LEU B  68     -26.605  37.217  17.764  1.00 42.11           C  
ANISOU 3071  CA  LEU B  68     4852   6456   4694    502   -510     73       C  
ATOM   3072  C   LEU B  68     -27.518  36.157  18.383  1.00 40.07           C  
ANISOU 3072  C   LEU B  68     4543   6209   4471    439   -543    -14       C  
ATOM   3073  O   LEU B  68     -28.057  36.307  19.483  1.00 40.17           O  
ANISOU 3073  O   LEU B  68     4544   6171   4548    413   -529    -16       O  
ATOM   3074  CB  LEU B  68     -26.177  38.262  18.793  1.00 32.13           C  
ANISOU 3074  CB  LEU B  68     3626   5087   3494    506   -456    139       C  
ATOM   3075  CG  LEU B  68     -25.141  39.316  18.398  1.00 36.45           C  
ANISOU 3075  CG  LEU B  68     4225   5594   4028    555   -410    223       C  
ATOM   3076  CD1 LEU B  68     -25.051  40.404  19.497  1.00 33.14           C  
ANISOU 3076  CD1 LEU B  68     3829   5082   3682    559   -361    278       C  
ATOM   3077  CD2 LEU B  68     -23.798  38.668  18.191  1.00 37.62           C  
ANISOU 3077  CD2 LEU B  68     4419   5703   4172    516   -394    203       C  
ATOM   3078  N   ARG B  69     -27.676  35.054  17.646  1.00 32.48           N  
ANISOU 3078  N   ARG B  69     3555   5315   3469    415   -583    -88       N  
ATOM   3079  CA  ARG B  69     -28.592  33.996  18.059  1.00 32.85           C  
ANISOU 3079  CA  ARG B  69     3550   5384   3549    357   -614   -175       C  
ATOM   3080  C   ARG B  69     -27.960  32.601  17.993  1.00 37.33           C  
ANISOU 3080  C   ARG B  69     4131   5929   4125    287   -619   -255       C  
ATOM   3081  O   ARG B  69     -28.668  31.607  17.883  1.00 36.43           O  
ANISOU 3081  O   ARG B  69     3969   5857   4016    247   -651   -337       O  
ATOM   3082  CB  ARG B  69     -29.879  34.068  17.245  1.00 37.72           C  
ANISOU 3082  CB  ARG B  69     4095   6124   4115    400   -668   -199       C  
ATOM   3083  CG  ARG B  69     -30.664  35.392  17.430  1.00 40.11           C  
ANISOU 3083  CG  ARG B  69     4376   6446   4419    468   -663   -122       C  
ATOM   3084  CD  ARG B  69     -31.251  35.575  18.851  1.00 42.51           C  
ANISOU 3084  CD  ARG B  69     4667   6673   4812    431   -637   -120       C  
ATOM   3085  NE  ARG B  69     -32.007  36.825  18.976  1.00 43.25           N  
ANISOU 3085  NE  ARG B  69     4739   6786   4906    498   -630    -50       N  
ATOM   3086  CZ  ARG B  69     -31.478  38.001  19.290  1.00 47.05           C  
ANISOU 3086  CZ  ARG B  69     5268   7207   5403    541   -585     38       C  
ATOM   3087  NH1 ARG B  69     -30.186  38.129  19.561  1.00 37.64           N  
ANISOU 3087  NH1 ARG B  69     4145   5930   4227    521   -543     65       N  
ATOM   3088  NH2 ARG B  69     -32.262  39.080  19.332  1.00 39.58           N  
ANISOU 3088  NH2 ARG B  69     4297   6285   4458    605   -579     97       N  
ATOM   3089  N   THR B  70     -26.627  32.497  18.103  1.00 32.30           N  
ANISOU 3089  N   THR B  70     3557   5222   3494    270   -583   -233       N  
ATOM   3090  CA  THR B  70     -26.000  31.184  18.264  1.00 31.20           C  
ANISOU 3090  CA  THR B  70     3434   5042   3378    201   -578   -303       C  
ATOM   3091  C   THR B  70     -26.136  30.695  19.707  1.00 34.56           C  
ANISOU 3091  C   THR B  70     3862   5377   3893    136   -552   -327       C  
ATOM   3092  O   THR B  70     -26.452  31.483  20.607  1.00 29.59           O  
ANISOU 3092  O   THR B  70     3234   4704   3303    146   -531   -280       O  
ATOM   3093  CB  THR B  70     -24.517  31.243  17.910  1.00 35.00           C  
ANISOU 3093  CB  THR B  70     3979   5480   3838    208   -548   -270       C  
ATOM   3094  OG1 THR B  70     -23.841  32.015  18.899  1.00 29.99           O  
ANISOU 3094  OG1 THR B  70     3389   4752   3256    207   -503   -205       O  
ATOM   3095  CG2 THR B  70     -24.285  31.869  16.538  1.00 36.57           C  
ANISOU 3095  CG2 THR B  70     4185   5762   3949    279   -563   -231       C  
ATOM   3096  N   PRO B  71     -25.903  29.391  19.956  1.00 31.25           N  
ANISOU 3096  N   PRO B  71     3443   4927   3504     71   -549   -398       N  
ATOM   3097  CA  PRO B  71     -25.938  28.899  21.346  1.00 34.32           C  
ANISOU 3097  CA  PRO B  71     3840   5226   3975     13   -518   -413       C  
ATOM   3098  C   PRO B  71     -25.039  29.689  22.276  1.00 31.47           C  
ANISOU 3098  C   PRO B  71     3534   4776   3645     21   -475   -342       C  
ATOM   3099  O   PRO B  71     -25.447  29.995  23.401  1.00 29.78           O  
ANISOU 3099  O   PRO B  71     3318   4514   3484      8   -455   -324       O  
ATOM   3100  CB  PRO B  71     -25.474  27.435  21.216  1.00 27.21           C  
ANISOU 3100  CB  PRO B  71     2945   4304   3090    -46   -515   -488       C  
ATOM   3101  CG  PRO B  71     -25.972  27.029  19.822  1.00 29.68           C  
ANISOU 3101  CG  PRO B  71     3216   4722   3338    -30   -561   -544       C  
ATOM   3102  CD  PRO B  71     -25.827  28.279  18.976  1.00 35.15           C  
ANISOU 3102  CD  PRO B  71     3919   5475   3960     48   -576   -475       C  
ATOM   3103  N   LEU B  72     -23.834  30.057  21.834  1.00 26.65           N  
ANISOU 3103  N   LEU B  72     2974   4147   3006     44   -459   -301       N  
ATOM   3104  CA  LEU B  72     -22.983  30.884  22.686  1.00 26.66           C  
ANISOU 3104  CA  LEU B  72     3023   4069   3040     52   -420   -236       C  
ATOM   3105  C   LEU B  72     -23.694  32.181  23.064  1.00 27.48           C  
ANISOU 3105  C   LEU B  72     3113   4178   3151     95   -416   -180       C  
ATOM   3106  O   LEU B  72     -23.687  32.585  24.229  1.00 26.14           O  
ANISOU 3106  O   LEU B  72     2958   3943   3032     81   -389   -157       O  
ATOM   3107  CB  LEU B  72     -21.671  31.190  21.966  1.00 24.21           C  
ANISOU 3107  CB  LEU B  72     2758   3748   2692     77   -405   -200       C  
ATOM   3108  CG  LEU B  72     -20.650  32.015  22.758  1.00 29.28           C  
ANISOU 3108  CG  LEU B  72     3448   4309   3369     82   -364   -140       C  
ATOM   3109  CD1 LEU B  72     -20.125  31.209  23.912  1.00 32.57           C  
ANISOU 3109  CD1 LEU B  72     3884   4648   3841     24   -343   -168       C  
ATOM   3110  CD2 LEU B  72     -19.500  32.450  21.864  1.00 35.43           C  
ANISOU 3110  CD2 LEU B  72     4262   5090   4108    114   -350   -101       C  
ATOM   3111  N   ASN B  73     -24.345  32.824  22.089  1.00 25.48           N  
ANISOU 3111  N   ASN B  73     2832   4005   2847    150   -441   -160       N  
ATOM   3112  CA  ASN B  73     -25.002  34.106  22.338  1.00 25.95           C  
ANISOU 3112  CA  ASN B  73     2879   4071   2912    199   -434   -101       C  
ATOM   3113  C   ASN B  73     -26.125  33.967  23.359  1.00 29.60           C  
ANISOU 3113  C   ASN B  73     3303   4519   3425    172   -437   -126       C  
ATOM   3114  O   ASN B  73     -26.298  34.833  24.222  1.00 26.70           O  
ANISOU 3114  O   ASN B  73     2946   4105   3095    185   -411    -83       O  
ATOM   3115  CB  ASN B  73     -25.560  34.690  21.033  1.00 24.65           C  
ANISOU 3115  CB  ASN B  73     2684   4005   2677    266   -465    -76       C  
ATOM   3116  CG  ASN B  73     -24.497  34.954  19.985  1.00 29.58           C  
ANISOU 3116  CG  ASN B  73     3347   4646   3246    302   -457    -42       C  
ATOM   3117  OD1 ASN B  73     -24.738  34.731  18.794  1.00 30.63           O  
ANISOU 3117  OD1 ASN B  73     3459   4868   3313    334   -489    -56       O  
ATOM   3118  ND2 ASN B  73     -23.322  35.421  20.408  1.00 28.40           N  
ANISOU 3118  ND2 ASN B  73     3252   4416   3124    297   -414      2       N  
ATOM   3119  N   TYR B  74     -26.939  32.912  23.245  1.00 27.60           N  
ANISOU 3119  N   TYR B  74     3004   4309   3176    137   -466   -196       N  
ATOM   3120  CA  TYR B  74     -28.010  32.711  24.217  1.00 25.11           C  
ANISOU 3120  CA  TYR B  74     2650   3978   2912    109   -464   -221       C  
ATOM   3121  C   TYR B  74     -27.458  32.449  25.605  1.00 22.54           C  
ANISOU 3121  C   TYR B  74     2363   3551   2650     62   -423   -220       C  
ATOM   3122  O   TYR B  74     -28.019  32.923  26.601  1.00 25.13           O  
ANISOU 3122  O   TYR B  74     2683   3844   3019     60   -404   -201       O  
ATOM   3123  CB  TYR B  74     -28.892  31.532  23.827  1.00 24.94           C  
ANISOU 3123  CB  TYR B  74     2571   4014   2890     73   -499   -303       C  
ATOM   3124  CG  TYR B  74     -29.907  31.838  22.797  1.00 33.43           C  
ANISOU 3124  CG  TYR B  74     3588   5197   3916    117   -544   -313       C  
ATOM   3125  CD1 TYR B  74     -31.092  32.476  23.130  1.00 37.32           C  
ANISOU 3125  CD1 TYR B  74     4033   5719   4426    144   -552   -296       C  
ATOM   3126  CD2 TYR B  74     -29.707  31.461  21.487  1.00 33.09           C  
ANISOU 3126  CD2 TYR B  74     3534   5230   3808    135   -579   -342       C  
ATOM   3127  CE1 TYR B  74     -32.048  32.744  22.166  1.00 48.53           C  
ANISOU 3127  CE1 TYR B  74     5394   7246   5799    189   -597   -306       C  
ATOM   3128  CE2 TYR B  74     -30.641  31.730  20.524  1.00 40.96           C  
ANISOU 3128  CE2 TYR B  74     4475   6336   4754    180   -624   -352       C  
ATOM   3129  CZ  TYR B  74     -31.810  32.368  20.863  1.00 41.85           C  
ANISOU 3129  CZ  TYR B  74     4538   6479   4883    208   -634   -334       C  
ATOM   3130  OH  TYR B  74     -32.741  32.616  19.874  1.00 42.76           O  
ANISOU 3130  OH  TYR B  74     4592   6710   4944    256   -683   -345       O  
ATOM   3131  N   ILE B  75     -26.391  31.643  25.699  1.00 23.47           N  
ANISOU 3131  N   ILE B  75     2520   3624   2774     23   -410   -241       N  
ATOM   3132  CA  ILE B  75     -25.819  31.312  27.002  1.00 25.87           C  
ANISOU 3132  CA  ILE B  75     2860   3839   3131    -19   -373   -240       C  
ATOM   3133  C   ILE B  75     -25.220  32.554  27.664  1.00 25.62           C  
ANISOU 3133  C   ILE B  75     2869   3754   3112     10   -343   -173       C  
ATOM   3134  O   ILE B  75     -25.384  32.765  28.874  1.00 24.11           O  
ANISOU 3134  O   ILE B  75     2687   3509   2964     -6   -318   -163       O  
ATOM   3135  CB  ILE B  75     -24.787  30.178  26.862  1.00 28.56           C  
ANISOU 3135  CB  ILE B  75     3231   4149   3473    -60   -366   -276       C  
ATOM   3136  CG1 ILE B  75     -25.472  28.868  26.458  1.00 34.78           C  
ANISOU 3136  CG1 ILE B  75     3976   4973   4266   -100   -386   -351       C  
ATOM   3137  CG2 ILE B  75     -24.027  29.964  28.165  1.00 28.32           C  
ANISOU 3137  CG2 ILE B  75     3242   4029   3488    -93   -328   -263       C  
ATOM   3138  CD1 ILE B  75     -26.357  28.302  27.525  1.00 38.04           C  
ANISOU 3138  CD1 ILE B  75     4362   5356   4737   -140   -371   -381       C  
ATOM   3139  N   LEU B  76     -24.528  33.406  26.890  1.00 25.29           N  
ANISOU 3139  N   LEU B  76     2852   3726   3033     54   -343   -128       N  
ATOM   3140  CA  LEU B  76     -23.976  34.627  27.485  1.00 22.52           C  
ANISOU 3140  CA  LEU B  76     2536   3321   2700     80   -312    -68       C  
ATOM   3141  C   LEU B  76     -25.081  35.600  27.863  1.00 22.62           C  
ANISOU 3141  C   LEU B  76     2520   3346   2727    113   -309    -40       C  
ATOM   3142  O   LEU B  76     -24.956  36.340  28.849  1.00 24.43           O  
ANISOU 3142  O   LEU B  76     2771   3520   2993    115   -279    -12       O  
ATOM   3143  CB  LEU B  76     -22.979  35.288  26.514  1.00 23.90           C  
ANISOU 3143  CB  LEU B  76     2741   3504   2836    118   -307    -25       C  
ATOM   3144  CG  LEU B  76     -21.502  34.919  26.787  1.00 27.09           C  
ANISOU 3144  CG  LEU B  76     3193   3847   3252     88   -285    -26       C  
ATOM   3145  CD1 LEU B  76     -21.010  35.544  28.092  1.00 28.54           C  
ANISOU 3145  CD1 LEU B  76     3407   3953   3485     74   -251     -3       C  
ATOM   3146  CD2 LEU B  76     -21.266  33.392  26.836  1.00 22.19           C  
ANISOU 3146  CD2 LEU B  76     2570   3227   2634     36   -297    -87       C  
ATOM   3147  N   LEU B  77     -26.174  35.610  27.099  1.00 24.53           N  
ANISOU 3147  N   LEU B  77     2714   3665   2942    140   -339    -49       N  
ATOM   3148  CA  LEU B  77     -27.331  36.399  27.502  1.00 22.06           C  
ANISOU 3148  CA  LEU B  77     2367   3367   2648    170   -337    -28       C  
ATOM   3149  C   LEU B  77     -27.888  35.905  28.830  1.00 25.89           C  
ANISOU 3149  C   LEU B  77     2842   3809   3187    124   -321    -60       C  
ATOM   3150  O   LEU B  77     -28.178  36.704  29.735  1.00 25.86           O  
ANISOU 3150  O   LEU B  77     2845   3764   3216    136   -294    -31       O  
ATOM   3151  CB  LEU B  77     -28.385  36.346  26.389  1.00 23.94           C  
ANISOU 3151  CB  LEU B  77     2548   3705   2843    206   -378    -39       C  
ATOM   3152  CG  LEU B  77     -29.717  37.021  26.744  1.00 32.44           C  
ANISOU 3152  CG  LEU B  77     3579   4808   3939    236   -380    -23       C  
ATOM   3153  CD1 LEU B  77     -29.548  38.501  27.003  1.00 33.67           C  
ANISOU 3153  CD1 LEU B  77     3760   4927   4104    289   -348     51       C  
ATOM   3154  CD2 LEU B  77     -30.693  36.808  25.598  1.00 31.15           C  
ANISOU 3154  CD2 LEU B  77     3355   4753   3730    268   -428    -43       C  
ATOM   3155  N   ASN B  78     -28.007  34.583  28.983  1.00 25.23           N  
ANISOU 3155  N   ASN B  78     2743   3728   3114     72   -333   -119       N  
ATOM   3156  CA  ASN B  78     -28.478  34.015  30.244  1.00 28.05           C  
ANISOU 3156  CA  ASN B  78     3093   4040   3523     28   -312   -147       C  
ATOM   3157  C   ASN B  78     -27.540  34.376  31.400  1.00 21.99           C  
ANISOU 3157  C   ASN B  78     2382   3188   2784     15   -273   -121       C  
ATOM   3158  O   ASN B  78     -27.994  34.746  32.492  1.00 24.66           O  
ANISOU 3158  O   ASN B  78     2721   3491   3157     11   -249   -111       O  
ATOM   3159  CB  ASN B  78     -28.588  32.499  30.098  1.00 28.30           C  
ANISOU 3159  CB  ASN B  78     3105   4085   3564    -24   -325   -212       C  
ATOM   3160  CG  ASN B  78     -29.286  31.839  31.284  1.00 27.34           C  
ANISOU 3160  CG  ASN B  78     2966   3926   3496    -66   -303   -242       C  
ATOM   3161  OD1 ASN B  78     -30.310  32.311  31.742  1.00 35.17           O  
ANISOU 3161  OD1 ASN B  78     3925   4928   4508    -53   -297   -234       O  
ATOM   3162  ND2 ASN B  78     -28.727  30.732  31.759  1.00 33.84           N  
ANISOU 3162  ND2 ASN B  78     3811   4706   4340   -115   -286   -274       N  
ATOM   3163  N   LEU B  79     -26.220  34.298  31.178  1.00 21.58           N  
ANISOU 3163  N   LEU B  79     2376   3107   2717      8   -267   -110       N  
ATOM   3164  CA  LEU B  79     -25.284  34.658  32.247  1.00 21.16           C  
ANISOU 3164  CA  LEU B  79     2372   2979   2688     -4   -234    -89       C  
ATOM   3165  C   LEU B  79     -25.424  36.130  32.629  1.00 22.48           C  
ANISOU 3165  C   LEU B  79     2550   3125   2865     37   -215    -41       C  
ATOM   3166  O   LEU B  79     -25.334  36.476  33.811  1.00 22.82           O  
ANISOU 3166  O   LEU B  79     2613   3118   2939     26   -188    -35       O  
ATOM   3167  CB  LEU B  79     -23.836  34.360  31.833  1.00 20.53           C  
ANISOU 3167  CB  LEU B  79     2334   2877   2590    -14   -233    -85       C  
ATOM   3168  CG  LEU B  79     -23.494  32.871  31.669  1.00 28.94           C  
ANISOU 3168  CG  LEU B  79     3399   3945   3654    -58   -243   -132       C  
ATOM   3169  CD1 LEU B  79     -22.074  32.716  31.172  1.00 27.81           C  
ANISOU 3169  CD1 LEU B  79     3294   3782   3491    -61   -240   -123       C  
ATOM   3170  CD2 LEU B  79     -23.661  32.142  32.985  1.00 26.16           C  
ANISOU 3170  CD2 LEU B  79     3053   3547   3340    -97   -221   -155       C  
ATOM   3171  N   ALA B  80     -25.640  37.008  31.643  1.00 23.66           N  
ANISOU 3171  N   ALA B  80     2687   3314   2989     85   -226     -7       N  
ATOM   3172  CA  ALA B  80     -25.830  38.429  31.943  1.00 22.48           C  
ANISOU 3172  CA  ALA B  80     2545   3142   2854    126   -202     40       C  
ATOM   3173  C   ALA B  80     -27.017  38.638  32.873  1.00 24.77           C  
ANISOU 3173  C   ALA B  80     2808   3428   3176    126   -191     33       C  
ATOM   3174  O   ALA B  80     -26.947  39.426  33.820  1.00 21.45           O  
ANISOU 3174  O   ALA B  80     2408   2957   2785    132   -160     51       O  
ATOM   3175  CB  ALA B  80     -26.029  39.216  30.645  1.00 22.77           C  
ANISOU 3175  CB  ALA B  80     2566   3230   2855    183   -215     80       C  
ATOM   3176  N   VAL B  81     -28.124  37.948  32.607  1.00 23.98           N  
ANISOU 3176  N   VAL B  81     2659   3381   3073    119   -215      4       N  
ATOM   3177  CA  VAL B  81     -29.300  38.066  33.463  1.00 22.16           C  
ANISOU 3177  CA  VAL B  81     2397   3149   2875    118   -203     -5       C  
ATOM   3178  C   VAL B  81     -29.005  37.524  34.852  1.00 22.56           C  
ANISOU 3178  C   VAL B  81     2475   3138   2959     72   -175    -29       C  
ATOM   3179  O   VAL B  81     -29.327  38.156  35.865  1.00 22.39           O  
ANISOU 3179  O   VAL B  81     2462   3080   2966     79   -146    -16       O  
ATOM   3180  CB  VAL B  81     -30.495  37.337  32.826  1.00 23.66           C  
ANISOU 3180  CB  VAL B  81     2524   3412   3056    115   -235    -38       C  
ATOM   3181  CG1 VAL B  81     -31.676  37.320  33.795  1.00 29.81           C  
ANISOU 3181  CG1 VAL B  81     3268   4183   3875    106   -219    -51       C  
ATOM   3182  CG2 VAL B  81     -30.855  37.998  31.490  1.00 23.23           C  
ANISOU 3182  CG2 VAL B  81     2440   3426   2962    171   -264     -9       C  
ATOM   3183  N   ALA B  82     -28.417  36.338  34.923  1.00 20.44           N  
ANISOU 3183  N   ALA B  82     2220   2860   2688     28   -182    -64       N  
ATOM   3184  CA  ALA B  82     -28.090  35.767  36.222  1.00 23.23           C  
ANISOU 3184  CA  ALA B  82     2600   3158   3068    -11   -156    -82       C  
ATOM   3185  C   ALA B  82     -27.127  36.675  36.992  1.00 19.75           C  
ANISOU 3185  C   ALA B  82     2211   2661   2633     -1   -130    -54       C  
ATOM   3186  O   ALA B  82     -27.282  36.880  38.198  1.00 23.13           O  
ANISOU 3186  O   ALA B  82     2653   3051   3084     -8   -103    -54       O  
ATOM   3187  CB  ALA B  82     -27.497  34.373  36.032  1.00 24.60           C  
ANISOU 3187  CB  ALA B  82     2782   3330   3236    -54   -166   -117       C  
ATOM   3188  N   ASP B  83     -26.155  37.269  36.291  1.00 20.36           N  
ANISOU 3188  N   ASP B  83     2314   2733   2690     18   -136    -30       N  
ATOM   3189  CA  ASP B  83     -25.246  38.218  36.933  1.00 22.51           C  
ANISOU 3189  CA  ASP B  83     2628   2952   2972     28   -112     -7       C  
ATOM   3190  C   ASP B  83     -26.002  39.410  37.516  1.00 23.74           C  
ANISOU 3190  C   ASP B  83     2777   3092   3150     59    -88     15       C  
ATOM   3191  O   ASP B  83     -25.652  39.909  38.588  1.00 23.12           O  
ANISOU 3191  O   ASP B  83     2727   2967   3092     53    -62     14       O  
ATOM   3192  CB  ASP B  83     -24.217  38.729  35.921  1.00 19.38           C  
ANISOU 3192  CB  ASP B  83     2252   2556   2555     47   -119     18       C  
ATOM   3193  CG  ASP B  83     -23.196  37.677  35.482  1.00 26.67           C  
ANISOU 3193  CG  ASP B  83     3193   3481   3460     16   -135     -2       C  
ATOM   3194  OD1 ASP B  83     -23.128  36.613  36.106  1.00 21.27           O  
ANISOU 3194  OD1 ASP B  83     2512   2788   2782    -20   -137    -34       O  
ATOM   3195  OD2 ASP B  83     -22.473  37.915  34.473  1.00 22.37           O  
ANISOU 3195  OD2 ASP B  83     2658   2948   2894     32   -144     16       O  
ATOM   3196  N   LEU B  84     -27.006  39.918  36.793  1.00 20.04           N  
ANISOU 3196  N   LEU B  84     2271   2664   2678     94    -97     34       N  
ATOM   3197  CA  LEU B  84     -27.761  41.061  37.297  1.00 20.94           C  
ANISOU 3197  CA  LEU B  84     2377   2764   2816    128    -72     57       C  
ATOM   3198  C   LEU B  84     -28.537  40.684  38.546  1.00 23.48           C  
ANISOU 3198  C   LEU B  84     2689   3071   3163    106    -54     32       C  
ATOM   3199  O   LEU B  84     -28.662  41.498  39.468  1.00 23.55           O  
ANISOU 3199  O   LEU B  84     2713   3040   3194    117    -23     40       O  
ATOM   3200  CB  LEU B  84     -28.707  41.595  36.218  1.00 22.14           C  
ANISOU 3200  CB  LEU B  84     2486   2970   2956    175    -86     86       C  
ATOM   3201  CG  LEU B  84     -27.932  42.352  35.122  1.00 25.23           C  
ANISOU 3201  CG  LEU B  84     2895   3366   3326    210    -90    125       C  
ATOM   3202  CD1 LEU B  84     -28.808  42.601  33.894  1.00 27.91           C  
ANISOU 3202  CD1 LEU B  84     3190   3776   3640    258   -113    151       C  
ATOM   3203  CD2 LEU B  84     -27.401  43.704  35.640  1.00 25.51           C  
ANISOU 3203  CD2 LEU B  84     2965   3338   3389    233    -49    157       C  
ATOM   3204  N   PHE B  85     -29.088  39.466  38.592  1.00 22.17           N  
ANISOU 3204  N   PHE B  85     2495   2933   2994     76    -70      1       N  
ATOM   3205  CA  PHE B  85     -29.706  39.005  39.838  1.00 20.59           C  
ANISOU 3205  CA  PHE B  85     2291   2713   2818     53    -47    -21       C  
ATOM   3206  C   PHE B  85     -28.680  38.924  40.955  1.00 23.53           C  
ANISOU 3206  C   PHE B  85     2716   3031   3194     29    -24    -30       C  
ATOM   3207  O   PHE B  85     -28.974  39.288  42.105  1.00 24.80           O  
ANISOU 3207  O   PHE B  85     2890   3163   3371     30      5    -33       O  
ATOM   3208  CB  PHE B  85     -30.390  37.639  39.649  1.00 20.35           C  
ANISOU 3208  CB  PHE B  85     2224   2719   2791     20    -62    -54       C  
ATOM   3209  CG  PHE B  85     -31.758  37.732  39.008  1.00 23.72           C  
ANISOU 3209  CG  PHE B  85     2588   3200   3226     42    -77    -54       C  
ATOM   3210  CD1 PHE B  85     -32.852  38.181  39.724  1.00 35.28           C  
ANISOU 3210  CD1 PHE B  85     4026   4662   4717     56    -53    -49       C  
ATOM   3211  CD2 PHE B  85     -31.927  37.403  37.670  1.00 32.88           C  
ANISOU 3211  CD2 PHE B  85     3715   4417   4363     49   -115    -60       C  
ATOM   3212  CE1 PHE B  85     -34.103  38.278  39.116  1.00 38.77           C  
ANISOU 3212  CE1 PHE B  85     4406   5158   5168     78    -68    -50       C  
ATOM   3213  CE2 PHE B  85     -33.166  37.489  37.069  1.00 32.56           C  
ANISOU 3213  CE2 PHE B  85     3612   4433   4326     71   -133    -63       C  
ATOM   3214  CZ  PHE B  85     -34.250  37.925  37.791  1.00 35.93           C  
ANISOU 3214  CZ  PHE B  85     4010   4858   4784     85   -110    -57       C  
ATOM   3215  N   MET B  86     -27.462  38.459  40.651  1.00 19.70           N  
ANISOU 3215  N   MET B  86     2262   2534   2690      9    -38    -36       N  
ATOM   3216  CA  MET B  86     -26.427  38.447  41.690  1.00 22.63           C  
ANISOU 3216  CA  MET B  86     2680   2859   3060    -10    -21    -44       C  
ATOM   3217  C   MET B  86     -26.153  39.852  42.211  1.00 26.85           C  
ANISOU 3217  C   MET B  86     3237   3358   3606     16      1    -28       C  
ATOM   3218  O   MET B  86     -26.030  40.066  43.424  1.00 25.06           O  
ANISOU 3218  O   MET B  86     3033   3100   3387      9     24    -40       O  
ATOM   3219  CB  MET B  86     -25.118  37.842  41.166  1.00 18.91           C  
ANISOU 3219  CB  MET B  86     2234   2382   2570    -30    -40    -50       C  
ATOM   3220  CG  MET B  86     -25.241  36.397  40.690  1.00 21.85           C  
ANISOU 3220  CG  MET B  86     2588   2781   2933    -58    -59    -70       C  
ATOM   3221  SD  MET B  86     -23.576  35.836  40.164  1.00 25.47           S  
ANISOU 3221  SD  MET B  86     3081   3227   3370    -76    -75    -74       S  
ATOM   3222  CE  MET B  86     -22.657  35.824  41.676  1.00 23.49           C  
ANISOU 3222  CE  MET B  86     2875   2929   3123    -91    -54    -81       C  
ATOM   3223  N   VAL B  87     -26.031  40.814  41.300  1.00 21.55           N  
ANISOU 3223  N   VAL B  87     2560   2690   2936     46     -3     -2       N  
ATOM   3224  CA  VAL B  87     -25.627  42.165  41.676  1.00 21.24           C  
ANISOU 3224  CA  VAL B  87     2546   2611   2914     68     22     12       C  
ATOM   3225  C   VAL B  87     -26.709  42.844  42.515  1.00 27.81           C  
ANISOU 3225  C   VAL B  87     3366   3432   3769     87     50     13       C  
ATOM   3226  O   VAL B  87     -26.425  43.397  43.583  1.00 24.10           O  
ANISOU 3226  O   VAL B  87     2922   2923   3311     84     76      0       O  
ATOM   3227  CB  VAL B  87     -25.283  42.983  40.413  1.00 25.09           C  
ANISOU 3227  CB  VAL B  87     3029   3104   3399     98     16     46       C  
ATOM   3228  CG1 VAL B  87     -25.220  44.487  40.731  1.00 25.60           C  
ANISOU 3228  CG1 VAL B  87     3108   3125   3493    128     50     65       C  
ATOM   3229  CG2 VAL B  87     -23.938  42.507  39.802  1.00 23.61           C  
ANISOU 3229  CG2 VAL B  87     2865   2914   3194     78     -2     43       C  
ATOM   3230  N   PHE B  88     -27.967  42.820  42.050  1.00 27.07           N  
ANISOU 3230  N   PHE B  88     3230   3376   3681    109     46     26       N  
ATOM   3231  CA  PHE B  88     -29.034  43.528  42.759  1.00 25.86           C  
ANISOU 3231  CA  PHE B  88     3062   3213   3551    132     76     31       C  
ATOM   3232  C   PHE B  88     -29.690  42.691  43.836  1.00 25.14           C  
ANISOU 3232  C   PHE B  88     2963   3125   3463    107     87      4       C  
ATOM   3233  O   PHE B  88     -30.101  43.241  44.859  1.00 27.61           O  
ANISOU 3233  O   PHE B  88     3285   3412   3793    116    119     -2       O  
ATOM   3234  CB  PHE B  88     -30.102  44.010  41.774  1.00 27.82           C  
ANISOU 3234  CB  PHE B  88     3264   3500   3805    173     68     62       C  
ATOM   3235  CG  PHE B  88     -29.585  45.045  40.834  1.00 36.21           C  
ANISOU 3235  CG  PHE B  88     4336   4553   4868    208     70     97       C  
ATOM   3236  CD1 PHE B  88     -29.411  46.356  41.256  1.00 37.58           C  
ANISOU 3236  CD1 PHE B  88     4532   4678   5068    234    107    114       C  
ATOM   3237  CD2 PHE B  88     -29.224  44.703  39.541  1.00 33.76           C  
ANISOU 3237  CD2 PHE B  88     4014   4280   4532    215     38    114       C  
ATOM   3238  CE1 PHE B  88     -28.892  47.312  40.388  1.00 43.33           C  
ANISOU 3238  CE1 PHE B  88     5270   5391   5802    267    115    151       C  
ATOM   3239  CE2 PHE B  88     -28.718  45.655  38.671  1.00 39.70           C  
ANISOU 3239  CE2 PHE B  88     4778   5024   5284    250     44    152       C  
ATOM   3240  CZ  PHE B  88     -28.546  46.954  39.088  1.00 40.71           C  
ANISOU 3240  CZ  PHE B  88     4928   5098   5442    276     85    173       C  
ATOM   3241  N   GLY B  89     -29.785  41.378  43.648  1.00 25.32           N  
ANISOU 3241  N   GLY B  89     2971   3177   3473     77     65    -13       N  
ATOM   3242  CA  GLY B  89     -30.434  40.549  44.654  1.00 25.39           C  
ANISOU 3242  CA  GLY B  89     2971   3186   3488     55     82    -34       C  
ATOM   3243  C   GLY B  89     -29.508  40.226  45.820  1.00 22.93           C  
ANISOU 3243  C   GLY B  89     2709   2838   3166     31     98    -53       C  
ATOM   3244  O   GLY B  89     -29.944  40.152  46.974  1.00 25.89           O  
ANISOU 3244  O   GLY B  89     3092   3198   3546     28    127    -63       O  
ATOM   3245  N   GLY B  90     -28.230  39.989  45.524  1.00 20.39           N  
ANISOU 3245  N   GLY B  90     2418   2505   2825     15     79    -57       N  
ATOM   3246  CA  GLY B  90     -27.315  39.593  46.590  1.00 20.83           C  
ANISOU 3246  CA  GLY B  90     2515   2535   2866     -6     89    -75       C  
ATOM   3247  C   GLY B  90     -26.299  40.627  47.033  1.00 24.11           C  
ANISOU 3247  C   GLY B  90     2968   2916   3277      3     96    -79       C  
ATOM   3248  O   GLY B  90     -26.162  40.883  48.241  1.00 20.49           O  
ANISOU 3248  O   GLY B  90     2534   2438   2814      2    117    -95       O  
ATOM   3249  N   PHE B  91     -25.616  41.272  46.073  1.00 20.16           N  
ANISOU 3249  N   PHE B  91     2471   2410   2780     12     80    -66       N  
ATOM   3250  CA  PHE B  91     -24.447  42.101  46.410  1.00 22.16           C  
ANISOU 3250  CA  PHE B  91     2758   2629   3034     11     84    -75       C  
ATOM   3251  C   PHE B  91     -24.841  43.375  47.124  1.00 24.42           C  
ANISOU 3251  C   PHE B  91     3051   2885   3340     33    116    -80       C  
ATOM   3252  O   PHE B  91     -24.046  43.922  47.913  1.00 20.69           O  
ANISOU 3252  O   PHE B  91     2608   2384   2868     27    127   -103       O  
ATOM   3253  CB  PHE B  91     -23.641  42.479  45.161  1.00 19.08           C  
ANISOU 3253  CB  PHE B  91     2368   2236   2647     16     66    -57       C  
ATOM   3254  CG  PHE B  91     -22.875  41.339  44.543  1.00 24.96           C  
ANISOU 3254  CG  PHE B  91     3114   3000   3368     -7     37    -59       C  
ATOM   3255  CD1 PHE B  91     -22.946  40.064  45.065  1.00 20.99           C  
ANISOU 3255  CD1 PHE B  91     2613   2514   2850    -31     29    -74       C  
ATOM   3256  CD2 PHE B  91     -22.064  41.560  43.423  1.00 21.89           C  
ANISOU 3256  CD2 PHE B  91     2727   2611   2978     -4     22    -43       C  
ATOM   3257  CE1 PHE B  91     -22.234  39.018  44.483  1.00 24.36           C  
ANISOU 3257  CE1 PHE B  91     3043   2954   3260    -51      6    -77       C  
ATOM   3258  CE2 PHE B  91     -21.344  40.503  42.831  1.00 20.85           C  
ANISOU 3258  CE2 PHE B  91     2597   2497   2826    -25     -3    -46       C  
ATOM   3259  CZ  PHE B  91     -21.438  39.231  43.362  1.00 22.21           C  
ANISOU 3259  CZ  PHE B  91     2771   2684   2984    -49    -11    -64       C  
ATOM   3260  N   THR B  92     -26.050  43.877  46.851  1.00 21.83           N  
ANISOU 3260  N   THR B  92     2696   2566   3032     59    132    -62       N  
ATOM   3261  CA  THR B  92     -26.547  45.004  47.622  1.00 22.56           C  
ANISOU 3261  CA  THR B  92     2795   2630   3146     81    167    -68       C  
ATOM   3262  C   THR B  92     -26.646  44.656  49.101  1.00 24.86           C  
ANISOU 3262  C   THR B  92     3107   2915   3424     68    185    -99       C  
ATOM   3263  O   THR B  92     -26.428  45.524  49.950  1.00 27.49           O  
ANISOU 3263  O   THR B  92     3462   3217   3765     74    209   -120       O  
ATOM   3264  CB  THR B  92     -27.910  45.449  47.096  1.00 23.51           C  
ANISOU 3264  CB  THR B  92     2878   2767   3289    114    180    -40       C  
ATOM   3265  OG1 THR B  92     -28.776  44.323  47.093  1.00 24.02           O  
ANISOU 3265  OG1 THR B  92     2914   2870   3342    103    168    -39       O  
ATOM   3266  CG2 THR B  92     -27.772  46.023  45.691  1.00 21.64           C  
ANISOU 3266  CG2 THR B  92     2625   2535   3062    137    167     -5       C  
ATOM   3267  N   THR B  93     -26.982  43.394  49.437  1.00 20.28           N  
ANISOU 3267  N   THR B  93     2520   2363   2822     50    176   -103       N  
ATOM   3268  CA  THR B  93     -26.923  42.996  50.846  1.00 22.45           C  
ANISOU 3268  CA  THR B  93     2819   2633   3076     40    194   -128       C  
ATOM   3269  C   THR B  93     -25.474  42.853  51.321  1.00 21.91           C  
ANISOU 3269  C   THR B  93     2788   2554   2983     21    178   -152       C  
ATOM   3270  O   THR B  93     -25.144  43.276  52.433  1.00 23.16           O  
ANISOU 3270  O   THR B  93     2973   2699   3129     23    194   -179       O  
ATOM   3271  CB  THR B  93     -27.720  41.701  51.096  1.00 22.05           C  
ANISOU 3271  CB  THR B  93     2751   2612   3017     28    197   -122       C  
ATOM   3272  OG1 THR B  93     -29.133  41.999  51.092  1.00 25.58           O  
ANISOU 3272  OG1 THR B  93     3164   3066   3487     48    221   -110       O  
ATOM   3273  CG2 THR B  93     -27.382  41.127  52.478  1.00 23.63           C  
ANISOU 3273  CG2 THR B  93     2983   2809   3186     18    213   -142       C  
ATOM   3274  N   THR B  94     -24.590  42.265  50.502  1.00 22.52           N  
ANISOU 3274  N   THR B  94     2866   2639   3052      4    146   -144       N  
ATOM   3275  CA  THR B  94     -23.185  42.156  50.902  1.00 21.44           C  
ANISOU 3275  CA  THR B  94     2759   2494   2894    -13    130   -166       C  
ATOM   3276  C   THR B  94     -22.595  43.519  51.240  1.00 23.87           C  
ANISOU 3276  C   THR B  94     3083   2769   3217     -5    141   -189       C  
ATOM   3277  O   THR B  94     -21.841  43.652  52.204  1.00 20.33           O  
ANISOU 3277  O   THR B  94     2659   2315   2750    -13    141   -221       O  
ATOM   3278  CB  THR B  94     -22.332  41.556  49.784  1.00 22.39           C  
ANISOU 3278  CB  THR B  94     2874   2623   3012    -28     98   -152       C  
ATOM   3279  OG1 THR B  94     -23.082  40.577  49.046  1.00 22.80           O  
ANISOU 3279  OG1 THR B  94     2900   2699   3063    -32     89   -130       O  
ATOM   3280  CG2 THR B  94     -21.040  40.955  50.393  1.00 18.86           C  
ANISOU 3280  CG2 THR B  94     2453   2178   2536    -47     81   -172       C  
ATOM   3281  N   LEU B  95     -22.908  44.532  50.424  1.00 20.85           N  
ANISOU 3281  N   LEU B  95     2686   2366   2869     10    152   -173       N  
ATOM   3282  CA  LEU B  95     -22.396  45.886  50.634  1.00 21.43           C  
ANISOU 3282  CA  LEU B  95     2773   2401   2969     17    170   -193       C  
ATOM   3283  C   LEU B  95     -22.910  46.480  51.934  1.00 23.82           C  
ANISOU 3283  C   LEU B  95     3089   2690   3270     27    200   -224       C  
ATOM   3284  O   LEU B  95     -22.136  47.007  52.746  1.00 21.38           O  
ANISOU 3284  O   LEU B  95     2803   2364   2958     18    205   -265       O  
ATOM   3285  CB  LEU B  95     -22.819  46.783  49.454  1.00 20.00           C  
ANISOU 3285  CB  LEU B  95     2572   2201   2827     39    182   -159       C  
ATOM   3286  CG  LEU B  95     -22.454  48.254  49.624  1.00 23.32           C  
ANISOU 3286  CG  LEU B  95     3004   2571   3285     48    211   -176       C  
ATOM   3287  CD1 LEU B  95     -20.956  48.371  49.726  1.00 26.23           C  
ANISOU 3287  CD1 LEU B  95     3392   2922   3653     22    196   -205       C  
ATOM   3288  CD2 LEU B  95     -22.937  49.017  48.446  1.00 29.11           C  
ANISOU 3288  CD2 LEU B  95     3719   3290   4054     76    226   -132       C  
ATOM   3289  N   TYR B  96     -24.230  46.442  52.133  1.00 21.56           N  
ANISOU 3289  N   TYR B  96     2788   2414   2990     46    222   -208       N  
ATOM   3290  CA  TYR B  96     -24.805  47.035  53.342  1.00 21.38           C  
ANISOU 3290  CA  TYR B  96     2778   2378   2966     59    255   -236       C  
ATOM   3291  C   TYR B  96     -24.257  46.355  54.592  1.00 24.70           C  
ANISOU 3291  C   TYR B  96     3225   2818   3340     44    248   -271       C  
ATOM   3292  O   TYR B  96     -23.893  47.026  55.564  1.00 23.00           O  
ANISOU 3292  O   TYR B  96     3032   2589   3118     45    263   -312       O  
ATOM   3293  CB  TYR B  96     -26.325  46.921  53.287  1.00 26.34           C  
ANISOU 3293  CB  TYR B  96     3381   3020   3606     81    278   -209       C  
ATOM   3294  CG  TYR B  96     -27.050  47.767  54.288  1.00 32.57           C  
ANISOU 3294  CG  TYR B  96     4178   3790   4406    101    320   -230       C  
ATOM   3295  CD1 TYR B  96     -27.290  49.110  54.045  1.00 38.73           C  
ANISOU 3295  CD1 TYR B  96     4956   4532   5229    122    348   -231       C  
ATOM   3296  CD2 TYR B  96     -27.501  47.224  55.479  1.00 38.24           C  
ANISOU 3296  CD2 TYR B  96     4909   4528   5094    102    336   -248       C  
ATOM   3297  CE1 TYR B  96     -27.957  49.893  54.975  1.00 52.16           C  
ANISOU 3297  CE1 TYR B  96     6665   6213   6942    142    390   -254       C  
ATOM   3298  CE2 TYR B  96     -28.174  47.995  56.412  1.00 35.13           C  
ANISOU 3298  CE2 TYR B  96     4524   4118   4707    122    377   -270       C  
ATOM   3299  CZ  TYR B  96     -28.401  49.326  56.158  1.00 42.92           C  
ANISOU 3299  CZ  TYR B  96     5507   5065   5737    141    403   -274       C  
ATOM   3300  OH  TYR B  96     -29.071  50.096  57.082  1.00 57.91           O  
ANISOU 3300  OH  TYR B  96     7415   6945   7645    161    446   -298       O  
ATOM   3301  N   THR B  97     -24.181  45.024  54.564  1.00 22.73           N  
ANISOU 3301  N   THR B  97     2973   2603   3060     32    226   -255       N  
ATOM   3302  CA  THR B  97     -23.615  44.237  55.658  1.00 20.40           C  
ANISOU 3302  CA  THR B  97     2703   2332   2717     22    218   -278       C  
ATOM   3303  C   THR B  97     -22.155  44.594  55.909  1.00 22.35           C  
ANISOU 3303  C   THR B  97     2970   2571   2950      8    195   -313       C  
ATOM   3304  O   THR B  97     -21.733  44.731  57.064  1.00 24.07           O  
ANISOU 3304  O   THR B  97     3211   2798   3136      9    198   -351       O  
ATOM   3305  CB  THR B  97     -23.756  42.749  55.316  1.00 21.97           C  
ANISOU 3305  CB  THR B  97     2892   2559   2895     12    202   -246       C  
ATOM   3306  OG1 THR B  97     -25.153  42.431  55.133  1.00 24.42           O  
ANISOU 3306  OG1 THR B  97     3178   2877   3223     22    225   -219       O  
ATOM   3307  CG2 THR B  97     -23.172  41.855  56.426  1.00 22.82           C  
ANISOU 3307  CG2 THR B  97     3026   2691   2952      8    197   -261       C  
ATOM   3308  N   SER B  98     -21.363  44.759  54.838  1.00 20.16           N  
ANISOU 3308  N   SER B  98     2684   2280   2696     -6    172   -304       N  
ATOM   3309  CA  SER B  98     -19.944  45.061  55.020  1.00 21.20           C  
ANISOU 3309  CA  SER B  98     2830   2405   2821    -22    150   -338       C  
ATOM   3310  C   SER B  98     -19.745  46.468  55.580  1.00 28.90           C  
ANISOU 3310  C   SER B  98     3814   3348   3819    -19    171   -383       C  
ATOM   3311  O   SER B  98     -18.813  46.710  56.358  1.00 23.68           O  
ANISOU 3311  O   SER B  98     3168   2691   3140    -30    159   -430       O  
ATOM   3312  CB  SER B  98     -19.195  44.904  53.685  1.00 24.68           C  
ANISOU 3312  CB  SER B  98     3257   2837   3285    -37    125   -314       C  
ATOM   3313  OG  SER B  98     -19.237  43.567  53.201  1.00 28.90           O  
ANISOU 3313  OG  SER B  98     3784   3400   3797    -42    104   -281       O  
ATOM   3314  N   LEU B  99     -20.592  47.413  55.169  1.00 21.92           N  
ANISOU 3314  N   LEU B  99     2919   2431   2978     -4    202   -371       N  
ATOM   3315  CA  LEU B  99     -20.536  48.769  55.697  1.00 25.99           C  
ANISOU 3315  CA  LEU B  99     3443   2908   3523      0    230   -413       C  
ATOM   3316  C   LEU B  99     -20.714  48.791  57.209  1.00 24.11           C  
ANISOU 3316  C   LEU B  99     3226   2689   3246      6    242   -460       C  
ATOM   3317  O   LEU B  99     -20.066  49.582  57.906  1.00 29.43           O  
ANISOU 3317  O   LEU B  99     3912   3346   3922     -2    247   -516       O  
ATOM   3318  CB  LEU B  99     -21.629  49.632  55.054  1.00 24.89           C  
ANISOU 3318  CB  LEU B  99     3288   2735   3432     23    266   -382       C  
ATOM   3319  CG  LEU B  99     -21.366  50.063  53.620  1.00 27.60           C  
ANISOU 3319  CG  LEU B  99     3615   3052   3821     24    264   -344       C  
ATOM   3320  CD1 LEU B  99     -22.615  50.741  53.095  1.00 28.29           C  
ANISOU 3320  CD1 LEU B  99     3686   3118   3945     55    299   -307       C  
ATOM   3321  CD2 LEU B  99     -20.197  51.033  53.617  1.00 27.01           C  
ANISOU 3321  CD2 LEU B  99     3550   2935   3780      6    270   -383       C  
ATOM   3322  N   HIS B 100     -21.648  47.989  57.730  1.00 27.89           N  
ANISOU 3322  N   HIS B 100     3707   3200   3690     21    250   -438       N  
ATOM   3323  CA  HIS B 100     -22.004  48.035  59.140  1.00 26.10           C  
ANISOU 3323  CA  HIS B 100     3501   2992   3424     33    269   -475       C  
ATOM   3324  C   HIS B 100     -21.285  47.001  59.988  1.00 30.21           C  
ANISOU 3324  C   HIS B 100     4039   3560   3878     27    241   -491       C  
ATOM   3325  O   HIS B 100     -21.305  47.107  61.233  1.00 27.66           O  
ANISOU 3325  O   HIS B 100     3737   3258   3514     38    252   -530       O  
ATOM   3326  CB  HIS B 100     -23.516  47.857  59.300  1.00 26.87           C  
ANISOU 3326  CB  HIS B 100     3590   3093   3525     57    305   -442       C  
ATOM   3327  CG  HIS B 100     -24.288  49.019  58.796  1.00 27.45           C  
ANISOU 3327  CG  HIS B 100     3650   3124   3657     72    339   -435       C  
ATOM   3328  ND1 HIS B 100     -24.512  50.139  59.562  1.00 35.61           N  
ANISOU 3328  ND1 HIS B 100     4697   4130   4705     83    373   -479       N  
ATOM   3329  CD2 HIS B 100     -24.830  49.270  57.582  1.00 33.38           C  
ANISOU 3329  CD2 HIS B 100     4374   3853   4455     79    344   -390       C  
ATOM   3330  CE1 HIS B 100     -25.190  51.022  58.852  1.00 35.68           C  
ANISOU 3330  CE1 HIS B 100     4687   4098   4770     98    401   -458       C  
ATOM   3331  NE2 HIS B 100     -25.391  50.522  57.646  1.00 31.35           N  
ANISOU 3331  NE2 HIS B 100     4116   3556   4241     97    383   -402       N  
ATOM   3332  N   GLY B 101     -20.653  46.020  59.358  1.00 27.25           N  
ANISOU 3332  N   GLY B 101     3658   3205   3492     14    207   -461       N  
ATOM   3333  CA  GLY B 101     -19.912  45.009  60.076  1.00 29.33           C  
ANISOU 3333  CA  GLY B 101     3937   3513   3696     12    181   -469       C  
ATOM   3334  C   GLY B 101     -20.731  43.856  60.609  1.00 30.82           C  
ANISOU 3334  C   GLY B 101     4133   3734   3845     29    196   -433       C  
ATOM   3335  O   GLY B 101     -20.229  43.117  61.467  1.00 25.79           O  
ANISOU 3335  O   GLY B 101     3514   3135   3152     36    183   -440       O  
ATOM   3336  N   TYR B 102     -21.970  43.687  60.153  1.00 24.58           N  
ANISOU 3336  N   TYR B 102     3327   2931   3082     37    223   -394       N  
ATOM   3337  CA  TYR B 102     -22.793  42.540  60.542  1.00 26.84           C  
ANISOU 3337  CA  TYR B 102     3615   3242   3342     48    242   -357       C  
ATOM   3338  C   TYR B 102     -24.082  42.573  59.722  1.00 26.71           C  
ANISOU 3338  C   TYR B 102     3570   3205   3374     51    266   -320       C  
ATOM   3339  O   TYR B 102     -24.399  43.565  59.060  1.00 22.64           O  
ANISOU 3339  O   TYR B 102     3039   2661   2904     51    272   -324       O  
ATOM   3340  CB  TYR B 102     -23.107  42.538  62.055  1.00 25.69           C  
ANISOU 3340  CB  TYR B 102     3495   3120   3145     72    269   -380       C  
ATOM   3341  CG  TYR B 102     -24.145  43.565  62.505  1.00 25.82           C  
ANISOU 3341  CG  TYR B 102     3512   3118   3182     88    310   -398       C  
ATOM   3342  CD1 TYR B 102     -23.853  44.920  62.523  1.00 29.23           C  
ANISOU 3342  CD1 TYR B 102     3945   3522   3638     86    311   -444       C  
ATOM   3343  CD2 TYR B 102     -25.396  43.165  62.942  1.00 29.92           C  
ANISOU 3343  CD2 TYR B 102     4027   3643   3698    106    351   -371       C  
ATOM   3344  CE1 TYR B 102     -24.802  45.866  62.952  1.00 32.38           C  
ANISOU 3344  CE1 TYR B 102     4346   3901   4058    103    353   -461       C  
ATOM   3345  CE2 TYR B 102     -26.356  44.095  63.367  1.00 29.77           C  
ANISOU 3345  CE2 TYR B 102     4007   3607   3699    123    392   -387       C  
ATOM   3346  CZ  TYR B 102     -26.053  45.439  63.363  1.00 34.95           C  
ANISOU 3346  CZ  TYR B 102     4667   4235   4378    123    392   -432       C  
ATOM   3347  OH  TYR B 102     -27.000  46.354  63.779  1.00 36.61           O  
ANISOU 3347  OH  TYR B 102     4876   4425   4610    142    435   -448       O  
ATOM   3348  N   PHE B 103     -24.830  41.475  59.781  1.00 23.73           N  
ANISOU 3348  N   PHE B 103     3184   2843   2988     54    282   -284       N  
ATOM   3349  CA  PHE B 103     -26.062  41.355  58.995  1.00 24.39           C  
ANISOU 3349  CA  PHE B 103     3234   2916   3117     54    301   -251       C  
ATOM   3350  C   PHE B 103     -27.168  42.141  59.681  1.00 27.17           C  
ANISOU 3350  C   PHE B 103     3584   3259   3480     76    344   -260       C  
ATOM   3351  O   PHE B 103     -27.937  41.620  60.487  1.00 26.62           O  
ANISOU 3351  O   PHE B 103     3519   3203   3393     88    378   -250       O  
ATOM   3352  CB  PHE B 103     -26.443  39.893  58.819  1.00 22.84           C  
ANISOU 3352  CB  PHE B 103     3026   2736   2914     45    305   -215       C  
ATOM   3353  CG  PHE B 103     -25.812  39.285  57.611  1.00 21.24           C  
ANISOU 3353  CG  PHE B 103     2809   2533   2728     23    267   -199       C  
ATOM   3354  CD1 PHE B 103     -26.378  39.482  56.368  1.00 25.55           C  
ANISOU 3354  CD1 PHE B 103     3319   3070   3319     15    258   -182       C  
ATOM   3355  CD2 PHE B 103     -24.599  38.612  57.703  1.00 22.19           C  
ANISOU 3355  CD2 PHE B 103     2949   2664   2817     12    240   -202       C  
ATOM   3356  CE1 PHE B 103     -25.781  38.969  55.217  1.00 24.92           C  
ANISOU 3356  CE1 PHE B 103     3227   2992   3251     -4    223   -170       C  
ATOM   3357  CE2 PHE B 103     -23.991  38.085  56.570  1.00 25.72           C  
ANISOU 3357  CE2 PHE B 103     3383   3110   3280     -7    207   -188       C  
ATOM   3358  CZ  PHE B 103     -24.584  38.260  55.316  1.00 26.50           C  
ANISOU 3358  CZ  PHE B 103     3448   3199   3422    -16    199   -173       C  
ATOM   3359  N   VAL B 104     -27.214  43.439  59.371  1.00 26.45           N  
ANISOU 3359  N   VAL B 104     3488   3142   3419     82    347   -280       N  
ATOM   3360  CA  VAL B 104     -28.233  44.307  59.942  1.00 25.51           C  
ANISOU 3360  CA  VAL B 104     3366   3010   3317    105    390   -291       C  
ATOM   3361  C   VAL B 104     -29.617  43.775  59.609  1.00 34.78           C  
ANISOU 3361  C   VAL B 104     4506   4190   4518    113    415   -252       C  
ATOM   3362  O   VAL B 104     -30.537  43.832  60.435  1.00 30.60           O  
ANISOU 3362  O   VAL B 104     3977   3664   3985    131    457   -253       O  
ATOM   3363  CB  VAL B 104     -28.056  45.742  59.424  1.00 35.38           C  
ANISOU 3363  CB  VAL B 104     4611   4224   4608    110    390   -311       C  
ATOM   3364  CG1 VAL B 104     -29.109  46.659  60.052  1.00 43.22           C  
ANISOU 3364  CG1 VAL B 104     5603   5200   5620    136    438   -323       C  
ATOM   3365  CG2 VAL B 104     -26.667  46.239  59.713  1.00 38.90           C  
ANISOU 3365  CG2 VAL B 104     5085   4662   5034     98    365   -353       C  
ATOM   3366  N   PHE B 105     -29.782  43.247  58.388  1.00 27.47           N  
ANISOU 3366  N   PHE B 105     3548   3268   3622     99    391   -221       N  
ATOM   3367  CA  PHE B 105     -31.050  42.699  57.914  1.00 31.62           C  
ANISOU 3367  CA  PHE B 105     4033   3803   4177    102    408   -189       C  
ATOM   3368  C   PHE B 105     -31.387  41.361  58.534  1.00 37.30           C  
ANISOU 3368  C   PHE B 105     4754   4544   4874     93    425   -175       C  
ATOM   3369  O   PHE B 105     -32.409  40.773  58.147  1.00 35.49           O  
ANISOU 3369  O   PHE B 105     4487   4323   4674     89    440   -152       O  
ATOM   3370  CB  PHE B 105     -31.036  42.472  56.401  1.00 43.11           C  
ANISOU 3370  CB  PHE B 105     5453   5263   5665     89    373   -166       C  
ATOM   3371  CG  PHE B 105     -30.702  43.666  55.594  1.00 46.87           C  
ANISOU 3371  CG  PHE B 105     5925   5719   6166     99    357   -168       C  
ATOM   3372  CD1 PHE B 105     -31.110  44.925  55.992  1.00 46.99           C  
ANISOU 3372  CD1 PHE B 105     5944   5710   6199    123    387   -180       C  
ATOM   3373  CD2 PHE B 105     -30.001  43.519  54.386  1.00 43.49           C  
ANISOU 3373  CD2 PHE B 105     5486   5293   5744     85    317   -156       C  
ATOM   3374  CE1 PHE B 105     -30.815  46.038  55.212  1.00 55.79           C  
ANISOU 3374  CE1 PHE B 105     7054   6801   7343    135    379   -178       C  
ATOM   3375  CE2 PHE B 105     -29.691  44.615  53.613  1.00 37.63           C  
ANISOU 3375  CE2 PHE B 105     4740   4530   5027     97    308   -153       C  
ATOM   3376  CZ  PHE B 105     -30.107  45.889  54.024  1.00 48.84           C  
ANISOU 3376  CZ  PHE B 105     6165   5923   6469    122    340   -162       C  
ATOM   3377  N   GLY B 106     -30.528  40.816  59.392  1.00 29.80           N  
ANISOU 3377  N   GLY B 106     3843   3603   3876     89    422   -186       N  
ATOM   3378  CA  GLY B 106     -30.819  39.557  60.034  1.00 28.27           C  
ANISOU 3378  CA  GLY B 106     3655   3425   3661     85    445   -168       C  
ATOM   3379  C   GLY B 106     -30.742  38.371  59.093  1.00 25.99           C  
ANISOU 3379  C   GLY B 106     3342   3143   3392     59    424   -143       C  
ATOM   3380  O   GLY B 106     -30.105  38.414  58.026  1.00 29.28           O  
ANISOU 3380  O   GLY B 106     3748   3556   3821     43    381   -144       O  
ATOM   3381  N   PRO B 107     -31.355  37.255  59.509  1.00 27.93           N  
ANISOU 3381  N   PRO B 107     3579   3394   3638     54    456   -122       N  
ATOM   3382  CA  PRO B 107     -31.304  36.045  58.677  1.00 24.27           C  
ANISOU 3382  CA  PRO B 107     3093   2932   3196     28    441   -103       C  
ATOM   3383  C   PRO B 107     -31.886  36.242  57.286  1.00 28.99           C  
ANISOU 3383  C   PRO B 107     3641   3531   3845     12    416   -101       C  
ATOM   3384  O   PRO B 107     -31.463  35.560  56.351  1.00 26.36           O  
ANISOU 3384  O   PRO B 107     3293   3200   3522    -10    385    -97       O  
ATOM   3385  CB  PRO B 107     -32.108  35.021  59.500  1.00 24.08           C  
ANISOU 3385  CB  PRO B 107     3065   2908   3175     29    494    -82       C  
ATOM   3386  CG  PRO B 107     -31.973  35.499  60.928  1.00 34.69           C  
ANISOU 3386  CG  PRO B 107     4452   4258   4471     59    526    -88       C  
ATOM   3387  CD  PRO B 107     -31.897  36.996  60.860  1.00 31.71           C  
ANISOU 3387  CD  PRO B 107     4078   3877   4091     74    508   -116       C  
ATOM   3388  N   THR B 108     -32.852  37.151  57.118  1.00 25.01           N  
ANISOU 3388  N   THR B 108     3108   3026   3370     27    429   -104       N  
ATOM   3389  CA  THR B 108     -33.367  37.416  55.782  1.00 27.25           C  
ANISOU 3389  CA  THR B 108     3342   3316   3694     20    402   -101       C  
ATOM   3390  C   THR B 108     -32.285  37.953  54.862  1.00 24.27           C  
ANISOU 3390  C   THR B 108     2978   2938   3306     16    352   -107       C  
ATOM   3391  O   THR B 108     -32.189  37.521  53.709  1.00 25.81           O  
ANISOU 3391  O   THR B 108     3146   3143   3517      0    320   -102       O  
ATOM   3392  CB  THR B 108     -34.539  38.384  55.852  1.00 31.47           C  
ANISOU 3392  CB  THR B 108     3847   3852   4259     44    427    -99       C  
ATOM   3393  OG1 THR B 108     -35.569  37.756  56.608  1.00 29.02           O  
ANISOU 3393  OG1 THR B 108     3519   3543   3963     44    475    -92       O  
ATOM   3394  CG2 THR B 108     -35.052  38.692  54.442  1.00 31.55           C  
ANISOU 3394  CG2 THR B 108     3805   3876   4305     43    395    -93       C  
ATOM   3395  N   GLY B 109     -31.460  38.886  55.354  1.00 25.06           N  
ANISOU 3395  N   GLY B 109     3117   3025   3381     31    346   -121       N  
ATOM   3396  CA  GLY B 109     -30.348  39.375  54.562  1.00 22.21           C  
ANISOU 3396  CA  GLY B 109     2769   2658   3011     26    304   -128       C  
ATOM   3397  C   GLY B 109     -29.346  38.285  54.232  1.00 22.61           C  
ANISOU 3397  C   GLY B 109     2834   2715   3041      1    276   -126       C  
ATOM   3398  O   GLY B 109     -28.825  38.224  53.111  1.00 23.03           O  
ANISOU 3398  O   GLY B 109     2876   2772   3103    -10    241   -122       O  
ATOM   3399  N   CYS B 110     -29.063  37.406  55.208  1.00 21.04           N  
ANISOU 3399  N   CYS B 110     2661   2519   2815     -4    294   -126       N  
ATOM   3400  CA  CYS B 110     -28.176  36.263  54.974  1.00 20.09           C  
ANISOU 3400  CA  CYS B 110     2554   2402   2676    -25    274   -120       C  
ATOM   3401  C   CYS B 110     -28.723  35.339  53.885  1.00 23.06           C  
ANISOU 3401  C   CYS B 110     2890   2786   3085    -47    264   -108       C  
ATOM   3402  O   CYS B 110     -27.969  34.861  53.038  1.00 21.19           O  
ANISOU 3402  O   CYS B 110     2652   2552   2847    -63    232   -108       O  
ATOM   3403  CB  CYS B 110     -27.999  35.493  56.292  1.00 22.81           C  
ANISOU 3403  CB  CYS B 110     2931   2750   2988    -19    304   -115       C  
ATOM   3404  SG  CYS B 110     -26.911  34.041  56.215  1.00 22.45           S  
ANISOU 3404  SG  CYS B 110     2904   2706   2919    -37    289   -103       S  
ATOM   3405  N   ASN B 111     -30.035  35.063  53.910  1.00 23.99           N  
ANISOU 3405  N   ASN B 111     2973   2908   3234    -48    293   -101       N  
ATOM   3406  CA  ASN B 111     -30.655  34.258  52.861  1.00 23.00           C  
ANISOU 3406  CA  ASN B 111     2802   2793   3143    -70    282    -98       C  
ATOM   3407  C   ASN B 111     -30.510  34.911  51.499  1.00 23.72           C  
ANISOU 3407  C   ASN B 111     2870   2898   3246    -69    239   -102       C  
ATOM   3408  O   ASN B 111     -30.227  34.224  50.516  1.00 22.51           O  
ANISOU 3408  O   ASN B 111     2699   2754   3099    -89    212   -105       O  
ATOM   3409  CB  ASN B 111     -32.140  34.026  53.156  1.00 23.31           C  
ANISOU 3409  CB  ASN B 111     2802   2837   3218    -70    321    -94       C  
ATOM   3410  CG  ASN B 111     -32.365  32.993  54.239  1.00 27.70           C  
ANISOU 3410  CG  ASN B 111     3374   3380   3771    -77    368    -85       C  
ATOM   3411  OD1 ASN B 111     -31.459  32.249  54.591  1.00 26.79           O  
ANISOU 3411  OD1 ASN B 111     3293   3256   3631    -85    368    -80       O  
ATOM   3412  ND2 ASN B 111     -33.584  32.942  54.772  1.00 29.90           N  
ANISOU 3412  ND2 ASN B 111     3625   3658   4076    -72    411    -81       N  
ATOM   3413  N   LEU B 112     -30.728  36.229  51.412  1.00 20.90           N  
ANISOU 3413  N   LEU B 112     2509   2540   2891    -45    235   -102       N  
ATOM   3414  CA  LEU B 112     -30.595  36.904  50.119  1.00 20.08           C  
ANISOU 3414  CA  LEU B 112     2383   2448   2796    -38    199    -99       C  
ATOM   3415  C   LEU B 112     -29.168  36.800  49.597  1.00 26.13           C  
ANISOU 3415  C   LEU B 112     3181   3209   3539    -48    165   -101       C  
ATOM   3416  O   LEU B 112     -28.944  36.524  48.413  1.00 21.06           O  
ANISOU 3416  O   LEU B 112     2520   2583   2900    -57    134    -99       O  
ATOM   3417  CB  LEU B 112     -30.978  38.382  50.237  1.00 26.93           C  
ANISOU 3417  CB  LEU B 112     3249   3309   3673     -6    209    -94       C  
ATOM   3418  CG  LEU B 112     -32.462  38.693  50.404  1.00 30.21           C  
ANISOU 3418  CG  LEU B 112     3625   3736   4119     11    236    -88       C  
ATOM   3419  CD1 LEU B 112     -32.579  40.109  50.860  1.00 27.30           C  
ANISOU 3419  CD1 LEU B 112     3270   3348   3754     43    254    -85       C  
ATOM   3420  CD2 LEU B 112     -33.222  38.471  49.084  1.00 29.08           C  
ANISOU 3420  CD2 LEU B 112     3425   3626   3999     10    210    -81       C  
ATOM   3421  N   GLU B 113     -28.194  37.076  50.462  1.00 20.14           N  
ANISOU 3421  N   GLU B 113     2467   2431   2755    -45    171   -108       N  
ATOM   3422  CA  GLU B 113     -26.800  37.078  50.037  1.00 20.27           C  
ANISOU 3422  CA  GLU B 113     2511   2441   2752    -54    141   -111       C  
ATOM   3423  C   GLU B 113     -26.384  35.688  49.578  1.00 19.59           C  
ANISOU 3423  C   GLU B 113     2420   2363   2659    -79    126   -110       C  
ATOM   3424  O   GLU B 113     -25.797  35.528  48.497  1.00 21.78           O  
ANISOU 3424  O   GLU B 113     2692   2648   2936    -88     96   -109       O  
ATOM   3425  CB  GLU B 113     -25.914  37.573  51.195  1.00 22.12           C  
ANISOU 3425  CB  GLU B 113     2788   2657   2960    -46    150   -124       C  
ATOM   3426  CG  GLU B 113     -24.697  38.403  50.797  1.00 19.69           C  
ANISOU 3426  CG  GLU B 113     2500   2336   2644    -44    126   -132       C  
ATOM   3427  CD  GLU B 113     -23.523  37.518  50.339  1.00 22.35           C  
ANISOU 3427  CD  GLU B 113     2849   2678   2964    -64     98   -131       C  
ATOM   3428  OE1 GLU B 113     -23.422  36.375  50.835  1.00 21.75           O  
ANISOU 3428  OE1 GLU B 113     2783   2610   2873    -75    104   -130       O  
ATOM   3429  OE2 GLU B 113     -22.714  37.972  49.492  1.00 20.47           O  
ANISOU 3429  OE2 GLU B 113     2613   2434   2730    -66     75   -130       O  
ATOM   3430  N   GLY B 114     -26.707  34.659  50.376  1.00 19.19           N  
ANISOU 3430  N   GLY B 114     2375   2311   2606    -90    151   -110       N  
ATOM   3431  CA  GLY B 114     -26.304  33.304  50.023  1.00 19.07           C  
ANISOU 3431  CA  GLY B 114     2360   2298   2590   -114    144   -109       C  
ATOM   3432  C   GLY B 114     -27.039  32.755  48.814  1.00 21.66           C  
ANISOU 3432  C   GLY B 114     2642   2642   2946   -130    131   -113       C  
ATOM   3433  O   GLY B 114     -26.440  32.116  47.938  1.00 18.98           O  
ANISOU 3433  O   GLY B 114     2299   2306   2604   -147    107   -117       O  
ATOM   3434  N   PHE B 115     -28.346  32.998  48.751  1.00 20.59           N  
ANISOU 3434  N   PHE B 115     2470   2518   2836   -126    146   -114       N  
ATOM   3435  CA  PHE B 115     -29.165  32.451  47.675  1.00 20.59           C  
ANISOU 3435  CA  PHE B 115     2420   2540   2863   -141    133   -123       C  
ATOM   3436  C   PHE B 115     -28.730  32.984  46.313  1.00 22.87           C  
ANISOU 3436  C   PHE B 115     2697   2850   3143   -135     89   -124       C  
ATOM   3437  O   PHE B 115     -28.560  32.209  45.362  1.00 21.00           O  
ANISOU 3437  O   PHE B 115     2442   2627   2909   -154     68   -136       O  
ATOM   3438  CB  PHE B 115     -30.643  32.780  47.922  1.00 22.93           C  
ANISOU 3438  CB  PHE B 115     2675   2848   3188   -132    156   -123       C  
ATOM   3439  CG  PHE B 115     -31.541  32.384  46.774  1.00 22.54           C  
ANISOU 3439  CG  PHE B 115     2568   2831   3166   -145    137   -138       C  
ATOM   3440  CD1 PHE B 115     -31.903  31.060  46.600  1.00 24.13           C  
ANISOU 3440  CD1 PHE B 115     2744   3032   3391   -178    148   -156       C  
ATOM   3441  CD2 PHE B 115     -31.997  33.335  45.857  1.00 27.63           C  
ANISOU 3441  CD2 PHE B 115     3181   3506   3812   -123    109   -134       C  
ATOM   3442  CE1 PHE B 115     -32.730  30.675  45.529  1.00 25.57           C  
ANISOU 3442  CE1 PHE B 115     2868   3249   3598   -193    126   -178       C  
ATOM   3443  CE2 PHE B 115     -32.829  32.957  44.776  1.00 24.92           C  
ANISOU 3443  CE2 PHE B 115     2780   3202   3487   -132     86   -151       C  
ATOM   3444  CZ  PHE B 115     -33.191  31.634  44.632  1.00 23.57           C  
ANISOU 3444  CZ  PHE B 115     2582   3034   3339   -168     94   -176       C  
ATOM   3445  N   PHE B 116     -28.560  34.311  46.184  1.00 19.39           N  
ANISOU 3445  N   PHE B 116     2264   2410   2692   -107     79   -113       N  
ATOM   3446  CA  PHE B 116     -28.282  34.825  44.852  1.00 22.42           C  
ANISOU 3446  CA  PHE B 116     2634   2816   3070    -97     44   -108       C  
ATOM   3447  C   PHE B 116     -26.855  34.526  44.409  1.00 20.30           C  
ANISOU 3447  C   PHE B 116     2398   2537   2777   -108     22   -109       C  
ATOM   3448  O   PHE B 116     -26.621  34.378  43.211  1.00 21.42           O  
ANISOU 3448  O   PHE B 116     2525   2701   2912   -110     -6   -110       O  
ATOM   3449  CB  PHE B 116     -28.593  36.323  44.762  1.00 22.51           C  
ANISOU 3449  CB  PHE B 116     2641   2828   3083    -61     45    -91       C  
ATOM   3450  CG  PHE B 116     -30.077  36.595  44.594  1.00 21.66           C  
ANISOU 3450  CG  PHE B 116     2485   2746   3000    -46     54    -88       C  
ATOM   3451  CD1 PHE B 116     -30.718  36.315  43.394  1.00 22.74           C  
ANISOU 3451  CD1 PHE B 116     2575   2926   3141    -45     27    -92       C  
ATOM   3452  CD2 PHE B 116     -30.830  37.074  45.657  1.00 26.43           C  
ANISOU 3452  CD2 PHE B 116     3087   3335   3618    -33     88    -86       C  
ATOM   3453  CE1 PHE B 116     -32.078  36.531  43.247  1.00 25.28           C  
ANISOU 3453  CE1 PHE B 116     2846   3276   3485    -30     32    -91       C  
ATOM   3454  CE2 PHE B 116     -32.186  37.294  45.522  1.00 26.58           C  
ANISOU 3454  CE2 PHE B 116     3058   3378   3662    -19     97    -83       C  
ATOM   3455  CZ  PHE B 116     -32.818  37.019  44.307  1.00 25.68           C  
ANISOU 3455  CZ  PHE B 116     2894   3308   3555    -18     68    -86       C  
ATOM   3456  N   ALA B 117     -25.897  34.419  45.343  1.00 21.56           N  
ANISOU 3456  N   ALA B 117     2600   2668   2923   -113     34   -109       N  
ATOM   3457  CA  ALA B 117     -24.549  34.027  44.927  1.00 19.13           C  
ANISOU 3457  CA  ALA B 117     2319   2352   2597   -125     14   -110       C  
ATOM   3458  C   ALA B 117     -24.507  32.556  44.511  1.00 20.50           C  
ANISOU 3458  C   ALA B 117     2483   2534   2774   -152      9   -122       C  
ATOM   3459  O   ALA B 117     -23.871  32.202  43.507  1.00 22.07           O  
ANISOU 3459  O   ALA B 117     2680   2742   2964   -160    -14   -126       O  
ATOM   3460  CB  ALA B 117     -23.539  34.298  46.056  1.00 21.08           C  
ANISOU 3460  CB  ALA B 117     2610   2572   2828   -122     25   -109       C  
ATOM   3461  N   THR B 118     -25.195  31.689  45.266  1.00 19.91           N  
ANISOU 3461  N   THR B 118     2400   2452   2714   -166     36   -128       N  
ATOM   3462  CA  THR B 118     -25.269  30.274  44.906  1.00 20.87           C  
ANISOU 3462  CA  THR B 118     2509   2573   2848   -194     40   -142       C  
ATOM   3463  C   THR B 118     -25.973  30.086  43.575  1.00 18.88           C  
ANISOU 3463  C   THR B 118     2212   2354   2609   -203     16   -159       C  
ATOM   3464  O   THR B 118     -25.509  29.334  42.708  1.00 21.53           O  
ANISOU 3464  O   THR B 118     2543   2697   2942   -220     -1   -173       O  
ATOM   3465  CB  THR B 118     -26.015  29.499  45.993  1.00 22.00           C  
ANISOU 3465  CB  THR B 118     2648   2699   3010   -205     81   -142       C  
ATOM   3466  OG1 THR B 118     -25.384  29.740  47.253  1.00 21.38           O  
ANISOU 3466  OG1 THR B 118     2613   2599   2912   -191    101   -127       O  
ATOM   3467  CG2 THR B 118     -26.017  27.984  45.681  1.00 19.56           C  
ANISOU 3467  CG2 THR B 118     2329   2381   2721   -236     92   -157       C  
ATOM   3468  N   LEU B 119     -27.111  30.763  43.403  1.00 20.00           N  
ANISOU 3468  N   LEU B 119     2318   2518   2764   -190     16   -159       N  
ATOM   3469  CA  LEU B 119     -27.855  30.651  42.152  1.00 22.00           C  
ANISOU 3469  CA  LEU B 119     2522   2811   3024   -193    -10   -176       C  
ATOM   3470  C   LEU B 119     -27.006  31.109  40.964  1.00 21.34           C  
ANISOU 3470  C   LEU B 119     2448   2748   2912   -180    -48   -171       C  
ATOM   3471  O   LEU B 119     -26.935  30.434  39.922  1.00 22.76           O  
ANISOU 3471  O   LEU B 119     2609   2952   3088   -194    -70   -191       O  
ATOM   3472  CB  LEU B 119     -29.134  31.486  42.268  1.00 19.68           C  
ANISOU 3472  CB  LEU B 119     2192   2540   2747   -172     -5   -170       C  
ATOM   3473  CG  LEU B 119     -30.012  31.500  41.018  1.00 27.24           C  
ANISOU 3473  CG  LEU B 119     3093   3548   3708   -169    -35   -186       C  
ATOM   3474  CD1 LEU B 119     -30.804  30.199  40.955  1.00 26.45           C  
ANISOU 3474  CD1 LEU B 119     2953   3457   3641   -206    -25   -222       C  
ATOM   3475  CD2 LEU B 119     -30.948  32.743  41.115  1.00 30.61           C  
ANISOU 3475  CD2 LEU B 119     3494   3995   4141   -132    -34   -167       C  
ATOM   3476  N   GLY B 120     -26.329  32.249  41.118  1.00 22.29           N  
ANISOU 3476  N   GLY B 120     2598   2856   3014   -153    -51   -145       N  
ATOM   3477  CA  GLY B 120     -25.523  32.769  40.026  1.00 22.97           C  
ANISOU 3477  CA  GLY B 120     2694   2958   3077   -138    -80   -135       C  
ATOM   3478  C   GLY B 120     -24.349  31.867  39.671  1.00 22.99           C  
ANISOU 3478  C   GLY B 120     2722   2949   3066   -160    -88   -146       C  
ATOM   3479  O   GLY B 120     -24.051  31.656  38.496  1.00 20.92           O  
ANISOU 3479  O   GLY B 120     2450   2712   2787   -160   -112   -152       O  
ATOM   3480  N   GLY B 121     -23.655  31.359  40.680  1.00 19.57           N  
ANISOU 3480  N   GLY B 121     2322   2478   2636   -175    -68   -146       N  
ATOM   3481  CA  GLY B 121     -22.536  30.457  40.445  1.00 21.87           C  
ANISOU 3481  CA  GLY B 121     2636   2755   2917   -193    -73   -153       C  
ATOM   3482  C   GLY B 121     -22.976  29.156  39.810  1.00 20.24           C  
ANISOU 3482  C   GLY B 121     2404   2563   2722   -220    -76   -181       C  
ATOM   3483  O   GLY B 121     -22.305  28.634  38.912  1.00 19.95           O  
ANISOU 3483  O   GLY B 121     2371   2535   2674   -229    -92   -192       O  
ATOM   3484  N   GLU B 122     -24.123  28.621  40.250  1.00 18.68           N  
ANISOU 3484  N   GLU B 122     2179   2368   2551   -234    -58   -196       N  
ATOM   3485  CA  GLU B 122     -24.615  27.374  39.676  1.00 20.61           C  
ANISOU 3485  CA  GLU B 122     2395   2623   2815   -264    -57   -230       C  
ATOM   3486  C   GLU B 122     -25.208  27.565  38.280  1.00 19.33           C  
ANISOU 3486  C   GLU B 122     2191   2512   2643   -261    -92   -251       C  
ATOM   3487  O   GLU B 122     -25.092  26.659  37.439  1.00 22.33           O  
ANISOU 3487  O   GLU B 122     2557   2905   3023   -282   -103   -282       O  
ATOM   3488  CB  GLU B 122     -25.626  26.719  40.633  1.00 21.39           C  
ANISOU 3488  CB  GLU B 122     2474   2702   2950   -283    -22   -239       C  
ATOM   3489  CG  GLU B 122     -24.933  26.053  41.842  1.00 21.73           C  
ANISOU 3489  CG  GLU B 122     2559   2697   3000   -291     15   -223       C  
ATOM   3490  CD  GLU B 122     -24.139  24.821  41.432  1.00 28.32           C  
ANISOU 3490  CD  GLU B 122     3408   3513   3840   -314     19   -238       C  
ATOM   3491  OE1 GLU B 122     -24.493  24.229  40.400  1.00 23.30           O  
ANISOU 3491  OE1 GLU B 122     2740   2896   3216   -334      6   -272       O  
ATOM   3492  OE2 GLU B 122     -23.157  24.452  42.115  1.00 22.96           O  
ANISOU 3492  OE2 GLU B 122     2769   2803   3153   -311     36   -219       O  
ATOM   3493  N   ILE B 123     -25.797  28.728  37.976  1.00 19.30           N  
ANISOU 3493  N   ILE B 123     2168   2539   2627   -231   -108   -235       N  
ATOM   3494  CA  ILE B 123     -26.211  28.955  36.591  1.00 19.58           C  
ANISOU 3494  CA  ILE B 123     2167   2630   2642   -219   -144   -250       C  
ATOM   3495  C   ILE B 123     -24.987  28.938  35.675  1.00 19.38           C  
ANISOU 3495  C   ILE B 123     2170   2610   2584   -213   -164   -245       C  
ATOM   3496  O   ILE B 123     -25.032  28.383  34.573  1.00 24.93           O  
ANISOU 3496  O   ILE B 123     2852   3349   3272   -221   -187   -273       O  
ATOM   3497  CB  ILE B 123     -27.007  30.262  36.452  1.00 19.75           C  
ANISOU 3497  CB  ILE B 123     2166   2683   2656   -181   -156   -226       C  
ATOM   3498  CG1 ILE B 123     -28.391  30.068  37.098  1.00 24.88           C  
ANISOU 3498  CG1 ILE B 123     2773   3339   3341   -192   -139   -240       C  
ATOM   3499  CG2 ILE B 123     -27.138  30.665  34.934  1.00 20.02           C  
ANISOU 3499  CG2 ILE B 123     2173   2778   2656   -156   -195   -228       C  
ATOM   3500  CD1 ILE B 123     -29.253  31.295  37.136  1.00 29.04           C  
ANISOU 3500  CD1 ILE B 123     3276   3891   3867   -154   -143   -216       C  
ATOM   3501  N   ALA B 124     -23.874  29.533  36.123  1.00 19.00           N  
ANISOU 3501  N   ALA B 124     2167   2527   2523   -198   -155   -213       N  
ATOM   3502  CA  ALA B 124     -22.656  29.515  35.313  1.00 22.89           C  
ANISOU 3502  CA  ALA B 124     2687   3022   2989   -193   -169   -206       C  
ATOM   3503  C   ALA B 124     -22.133  28.088  35.119  1.00 19.28           C  
ANISOU 3503  C   ALA B 124     2236   2550   2538   -227   -164   -238       C  
ATOM   3504  O   ALA B 124     -21.729  27.708  34.014  1.00 21.60           O  
ANISOU 3504  O   ALA B 124     2527   2869   2811   -229   -183   -254       O  
ATOM   3505  CB  ALA B 124     -21.584  30.414  35.962  1.00 18.45           C  
ANISOU 3505  CB  ALA B 124     2167   2422   2421   -175   -157   -170       C  
ATOM   3506  N   LEU B 125     -22.090  27.291  36.187  1.00 20.97           N  
ANISOU 3506  N   LEU B 125     2463   2723   2780   -251   -137   -245       N  
ATOM   3507  CA  LEU B 125     -21.546  25.935  36.070  1.00 19.04           C  
ANISOU 3507  CA  LEU B 125     2229   2458   2547   -281   -125   -271       C  
ATOM   3508  C   LEU B 125     -22.365  25.102  35.095  1.00 19.12           C  
ANISOU 3508  C   LEU B 125     2198   2502   2565   -303   -138   -318       C  
ATOM   3509  O   LEU B 125     -21.834  24.493  34.162  1.00 21.88           O  
ANISOU 3509  O   LEU B 125     2548   2863   2901   -312   -150   -341       O  
ATOM   3510  CB  LEU B 125     -21.502  25.255  37.459  1.00 19.92           C  
ANISOU 3510  CB  LEU B 125     2359   2520   2689   -298    -88   -264       C  
ATOM   3511  CG  LEU B 125     -20.947  23.807  37.483  1.00 25.08           C  
ANISOU 3511  CG  LEU B 125     3025   3142   3361   -326    -67   -284       C  
ATOM   3512  CD1 LEU B 125     -19.592  23.704  36.754  1.00 23.33           C  
ANISOU 3512  CD1 LEU B 125     2831   2919   3114   -319    -81   -280       C  
ATOM   3513  CD2 LEU B 125     -20.827  23.266  38.891  1.00 28.18           C  
ANISOU 3513  CD2 LEU B 125     3441   3489   3777   -332    -28   -266       C  
ATOM   3514  N   TRP B 126     -23.673  25.083  35.284  1.00 19.43           N  
ANISOU 3514  N   TRP B 126     2197   2560   2627   -311   -136   -335       N  
ATOM   3515  CA  TRP B 126     -24.510  24.303  34.401  1.00 19.90           C  
ANISOU 3515  CA  TRP B 126     2210   2655   2697   -334   -150   -387       C  
ATOM   3516  C   TRP B 126     -24.540  24.907  33.002  1.00 23.71           C  
ANISOU 3516  C   TRP B 126     2673   3201   3135   -310   -193   -395       C  
ATOM   3517  O   TRP B 126     -24.701  24.174  32.022  1.00 23.46           O  
ANISOU 3517  O   TRP B 126     2616   3200   3096   -327   -210   -441       O  
ATOM   3518  CB  TRP B 126     -25.900  24.190  35.033  1.00 22.92           C  
ANISOU 3518  CB  TRP B 126     2550   3040   3117   -348   -135   -402       C  
ATOM   3519  CG  TRP B 126     -25.903  23.232  36.195  1.00 21.97           C  
ANISOU 3519  CG  TRP B 126     2445   2860   3043   -378    -87   -403       C  
ATOM   3520  CD1 TRP B 126     -25.946  23.535  37.551  1.00 24.77           C  
ANISOU 3520  CD1 TRP B 126     2823   3174   3413   -369    -54   -366       C  
ATOM   3521  CD2 TRP B 126     -25.839  21.804  36.108  1.00 23.71           C  
ANISOU 3521  CD2 TRP B 126     2660   3051   3298   -418    -63   -442       C  
ATOM   3522  NE1 TRP B 126     -25.945  22.364  38.285  1.00 22.36           N  
ANISOU 3522  NE1 TRP B 126     2527   2822   3148   -399    -11   -377       N  
ATOM   3523  CE2 TRP B 126     -25.854  21.298  37.423  1.00 23.21           C  
ANISOU 3523  CE2 TRP B 126     2617   2930   3270   -429    -14   -422       C  
ATOM   3524  CE3 TRP B 126     -25.745  20.904  35.030  1.00 26.64           C  
ANISOU 3524  CE3 TRP B 126     3011   3438   3671   -443    -76   -494       C  
ATOM   3525  CZ2 TRP B 126     -25.820  19.929  37.694  1.00 23.46           C  
ANISOU 3525  CZ2 TRP B 126     2650   2918   3346   -464     26   -446       C  
ATOM   3526  CZ3 TRP B 126     -25.699  19.544  35.300  1.00 26.81           C  
ANISOU 3526  CZ3 TRP B 126     3034   3413   3740   -482    -38   -524       C  
ATOM   3527  CH2 TRP B 126     -25.721  19.072  36.624  1.00 23.29           C  
ANISOU 3527  CH2 TRP B 126     2609   2907   3333   -491     14   -497       C  
ATOM   3528  N   SER B 127     -24.306  26.225  32.867  1.00 21.34           N  
ANISOU 3528  N   SER B 127     2386   2919   2802   -269   -209   -351       N  
ATOM   3529  CA  SER B 127     -24.151  26.789  31.519  1.00 20.08           C  
ANISOU 3529  CA  SER B 127     2216   2817   2596   -240   -244   -349       C  
ATOM   3530  C   SER B 127     -22.910  26.231  30.817  1.00 23.41           C  
ANISOU 3530  C   SER B 127     2670   3230   2995   -246   -248   -358       C  
ATOM   3531  O   SER B 127     -22.918  26.052  29.595  1.00 24.89           O  
ANISOU 3531  O   SER B 127     2841   3467   3149   -239   -274   -382       O  
ATOM   3532  CB  SER B 127     -24.044  28.323  31.562  1.00 22.34           C  
ANISOU 3532  CB  SER B 127     2516   3113   2859   -193   -251   -294       C  
ATOM   3533  OG  SER B 127     -25.283  28.935  31.874  1.00 22.21           O  
ANISOU 3533  OG  SER B 127     2463   3121   2856   -179   -255   -288       O  
ATOM   3534  N   LEU B 128     -21.820  26.021  31.569  1.00 23.44           N  
ANISOU 3534  N   LEU B 128     2718   3174   3011   -256   -222   -336       N  
ATOM   3535  CA  LEU B 128     -20.619  25.415  30.996  1.00 22.30           C  
ANISOU 3535  CA  LEU B 128     2604   3018   2852   -263   -220   -344       C  
ATOM   3536  C   LEU B 128     -20.881  23.976  30.561  1.00 25.49           C  
ANISOU 3536  C   LEU B 128     2988   3424   3273   -300   -216   -403       C  
ATOM   3537  O   LEU B 128     -20.349  23.534  29.539  1.00 25.99           O  
ANISOU 3537  O   LEU B 128     3055   3508   3311   -302   -228   -426       O  
ATOM   3538  CB  LEU B 128     -19.451  25.469  31.992  1.00 22.25           C  
ANISOU 3538  CB  LEU B 128     2644   2950   2860   -264   -193   -309       C  
ATOM   3539  CG  LEU B 128     -18.956  26.858  32.444  1.00 23.71           C  
ANISOU 3539  CG  LEU B 128     2852   3123   3032   -231   -193   -257       C  
ATOM   3540  CD1 LEU B 128     -17.829  26.727  33.501  1.00 25.54           C  
ANISOU 3540  CD1 LEU B 128     3124   3298   3280   -238   -169   -234       C  
ATOM   3541  CD2 LEU B 128     -18.472  27.670  31.229  1.00 32.00           C  
ANISOU 3541  CD2 LEU B 128     3905   4210   4042   -200   -213   -238       C  
ATOM   3542  N   VAL B 129     -21.678  23.228  31.341  1.00 22.91           N  
ANISOU 3542  N   VAL B 129     2641   3072   2990   -332   -196   -428       N  
ATOM   3543  CA  VAL B 129     -22.124  21.895  30.925  1.00 20.25           C  
ANISOU 3543  CA  VAL B 129     2278   2737   2679   -371   -189   -490       C  
ATOM   3544  C   VAL B 129     -22.836  21.970  29.579  1.00 25.22           C  
ANISOU 3544  C   VAL B 129     2864   3442   3278   -366   -229   -533       C  
ATOM   3545  O   VAL B 129     -22.558  21.188  28.667  1.00 27.29           O  
ANISOU 3545  O   VAL B 129     3120   3720   3527   -381   -238   -578       O  
ATOM   3546  CB  VAL B 129     -23.044  21.279  32.001  1.00 22.03           C  
ANISOU 3546  CB  VAL B 129     2484   2926   2962   -401   -158   -504       C  
ATOM   3547  CG1 VAL B 129     -23.729  19.998  31.459  1.00 27.12           C  
ANISOU 3547  CG1 VAL B 129     3088   3577   3639   -444   -152   -576       C  
ATOM   3548  CG2 VAL B 129     -22.267  20.990  33.237  1.00 22.20           C  
ANISOU 3548  CG2 VAL B 129     2549   2878   3008   -405   -118   -466       C  
ATOM   3549  N   VAL B 130     -23.760  22.919  29.431  1.00 22.65           N  
ANISOU 3549  N   VAL B 130     2507   3165   2935   -341   -254   -521       N  
ATOM   3550  CA  VAL B 130     -24.484  23.059  28.167  1.00 24.81           C  
ANISOU 3550  CA  VAL B 130     2735   3520   3172   -329   -296   -558       C  
ATOM   3551  C   VAL B 130     -23.523  23.374  27.023  1.00 26.59           C  
ANISOU 3551  C   VAL B 130     2986   3780   3338   -300   -318   -548       C  
ATOM   3552  O   VAL B 130     -23.632  22.812  25.923  1.00 27.28           O  
ANISOU 3552  O   VAL B 130     3051   3915   3398   -307   -341   -599       O  
ATOM   3553  CB  VAL B 130     -25.570  24.138  28.295  1.00 23.10           C  
ANISOU 3553  CB  VAL B 130     2483   3348   2948   -299   -316   -534       C  
ATOM   3554  CG1 VAL B 130     -26.200  24.399  26.927  1.00 27.58           C  
ANISOU 3554  CG1 VAL B 130     3005   4008   3465   -276   -364   -564       C  
ATOM   3555  CG2 VAL B 130     -26.666  23.633  29.279  1.00 25.80           C  
ANISOU 3555  CG2 VAL B 130     2789   3663   3351   -334   -294   -559       C  
ATOM   3556  N   LEU B 131     -22.591  24.304  27.250  1.00 24.16           N  
ANISOU 3556  N   LEU B 131     2722   3449   3008   -266   -310   -483       N  
ATOM   3557  CA  LEU B 131     -21.642  24.665  26.189  1.00 24.96           C  
ANISOU 3557  CA  LEU B 131     2848   3579   3056   -236   -325   -467       C  
ATOM   3558  C   LEU B 131     -20.705  23.516  25.854  1.00 27.26           C  
ANISOU 3558  C   LEU B 131     3164   3842   3351   -265   -310   -502       C  
ATOM   3559  O   LEU B 131     -20.341  23.322  24.687  1.00 27.51           O  
ANISOU 3559  O   LEU B 131     3196   3917   3340   -253   -328   -524       O  
ATOM   3560  CB  LEU B 131     -20.818  25.895  26.589  1.00 21.91           C  
ANISOU 3560  CB  LEU B 131     2503   3165   2657   -199   -313   -392       C  
ATOM   3561  CG  LEU B 131     -21.598  27.211  26.639  1.00 30.04           C  
ANISOU 3561  CG  LEU B 131     3513   4228   3673   -159   -327   -351       C  
ATOM   3562  CD1 LEU B 131     -20.737  28.304  27.255  1.00 30.50           C  
ANISOU 3562  CD1 LEU B 131     3614   4241   3736   -134   -306   -285       C  
ATOM   3563  CD2 LEU B 131     -22.075  27.622  25.249  1.00 34.54           C  
ANISOU 3563  CD2 LEU B 131     4054   4884   4185   -122   -363   -358       C  
ATOM   3564  N   ALA B 132     -20.270  22.765  26.860  1.00 23.50           N  
ANISOU 3564  N   ALA B 132     2711   3294   2926   -298   -275   -504       N  
ATOM   3565  CA  ALA B 132     -19.385  21.636  26.579  1.00 24.92           C  
ANISOU 3565  CA  ALA B 132     2912   3442   3114   -324   -257   -536       C  
ATOM   3566  C   ALA B 132     -20.090  20.610  25.706  1.00 27.00           C  
ANISOU 3566  C   ALA B 132     3137   3744   3377   -352   -271   -615       C  
ATOM   3567  O   ALA B 132     -19.491  20.031  24.794  1.00 30.31           O  
ANISOU 3567  O   ALA B 132     3566   4177   3772   -356   -274   -647       O  
ATOM   3568  CB  ALA B 132     -18.906  20.992  27.887  1.00 22.74           C  
ANISOU 3568  CB  ALA B 132     2664   3084   2894   -350   -216   -521       C  
ATOM   3569  N   ILE B 133     -21.375  20.376  25.965  1.00 24.79           N  
ANISOU 3569  N   ILE B 133     2812   3482   3126   -374   -278   -650       N  
ATOM   3570  CA  ILE B 133     -22.124  19.433  25.135  1.00 28.17           C  
ANISOU 3570  CA  ILE B 133     3195   3950   3557   -404   -294   -734       C  
ATOM   3571  C   ILE B 133     -22.315  19.985  23.733  1.00 31.93           C  
ANISOU 3571  C   ILE B 133     3651   4520   3961   -370   -341   -751       C  
ATOM   3572  O   ILE B 133     -22.205  19.251  22.743  1.00 32.13           O  
ANISOU 3572  O   ILE B 133     3665   4580   3964   -383   -354   -812       O  
ATOM   3573  CB  ILE B 133     -23.463  19.104  25.805  1.00 30.86           C  
ANISOU 3573  CB  ILE B 133     3487   4286   3950   -436   -288   -766       C  
ATOM   3574  CG1 ILE B 133     -23.206  18.244  27.044  1.00 33.14           C  
ANISOU 3574  CG1 ILE B 133     3800   4482   4311   -473   -234   -760       C  
ATOM   3575  CG2 ILE B 133     -24.435  18.460  24.793  1.00 32.89           C  
ANISOU 3575  CG2 ILE B 133     3685   4610   4202   -460   -318   -855       C  
ATOM   3576  CD1 ILE B 133     -24.354  18.207  27.981  1.00 35.14           C  
ANISOU 3576  CD1 ILE B 133     4018   4718   4617   -493   -218   -764       C  
ATOM   3577  N   GLU B 134     -22.604  21.285  23.624  1.00 33.15           N  
ANISOU 3577  N   GLU B 134     3800   4720   4077   -324   -366   -698       N  
ATOM   3578  CA  GLU B 134     -22.771  21.913  22.316  1.00 36.58           C  
ANISOU 3578  CA  GLU B 134     4217   5245   4436   -281   -409   -702       C  
ATOM   3579  C   GLU B 134     -21.493  21.814  21.488  1.00 34.05           C  
ANISOU 3579  C   GLU B 134     3941   4927   4071   -263   -404   -692       C  
ATOM   3580  O   GLU B 134     -21.531  21.472  20.297  1.00 37.64           O  
ANISOU 3580  O   GLU B 134     4379   5446   4475   -255   -430   -738       O  
ATOM   3581  CB  GLU B 134     -23.181  23.382  22.483  1.00 33.47           C  
ANISOU 3581  CB  GLU B 134     3818   4883   4016   -230   -425   -632       C  
ATOM   3582  CG  GLU B 134     -23.478  24.078  21.134  1.00 28.05           C  
ANISOU 3582  CG  GLU B 134     3111   4298   3250   -179   -468   -629       C  
ATOM   3583  CD  GLU B 134     -22.325  24.944  20.629  1.00 34.66           C  
ANISOU 3583  CD  GLU B 134     3998   5135   4037   -130   -461   -561       C  
ATOM   3584  OE1 GLU B 134     -21.280  24.995  21.299  1.00 34.94           O  
ANISOU 3584  OE1 GLU B 134     4081   5093   4101   -139   -425   -522       O  
ATOM   3585  OE2 GLU B 134     -22.470  25.573  19.555  1.00 37.19           O  
ANISOU 3585  OE2 GLU B 134     4306   5533   4290    -81   -489   -547       O  
ATOM   3586  N   ARG B 135     -20.346  22.122  22.102  1.00 25.28           N  
ANISOU 3586  N   ARG B 135     2882   3748   2974   -255   -372   -632       N  
ATOM   3587  CA  ARG B 135     -19.074  21.969  21.395  1.00 29.81           C  
ANISOU 3587  CA  ARG B 135     3496   4316   3513   -241   -362   -622       C  
ATOM   3588  C   ARG B 135     -18.834  20.523  20.974  1.00 40.06           C  
ANISOU 3588  C   ARG B 135     4792   5601   4826   -283   -351   -698       C  
ATOM   3589  O   ARG B 135     -18.318  20.264  19.878  1.00 38.48           O  
ANISOU 3589  O   ARG B 135     4602   5440   4579   -270   -360   -723       O  
ATOM   3590  CB  ARG B 135     -17.923  22.446  22.282  1.00 27.55           C  
ANISOU 3590  CB  ARG B 135     3260   3954   3252   -232   -327   -552       C  
ATOM   3591  CG  ARG B 135     -17.894  23.967  22.524  1.00 30.34           C  
ANISOU 3591  CG  ARG B 135     3624   4317   3586   -187   -333   -476       C  
ATOM   3592  CD  ARG B 135     -17.575  24.730  21.228  1.00 34.30           C  
ANISOU 3592  CD  ARG B 135     4131   4884   4016   -137   -352   -451       C  
ATOM   3593  NE  ARG B 135     -18.765  25.033  20.436  1.00 30.92           N  
ANISOU 3593  NE  ARG B 135     3660   4544   3546   -113   -391   -474       N  
ATOM   3594  CZ  ARG B 135     -18.720  25.493  19.196  1.00 35.75           C  
ANISOU 3594  CZ  ARG B 135     4267   5229   4088    -69   -412   -466       C  
ATOM   3595  NH1 ARG B 135     -17.563  25.670  18.572  1.00 33.55           N  
ANISOU 3595  NH1 ARG B 135     4027   4944   3776    -46   -396   -437       N  
ATOM   3596  NH2 ARG B 135     -19.856  25.799  18.576  1.00 33.77           N  
ANISOU 3596  NH2 ARG B 135     3972   5060   3798    -45   -450   -484       N  
ATOM   3597  N   TYR B 136     -19.168  19.571  21.851  1.00 35.99           N  
ANISOU 3597  N   TYR B 136     4267   5028   4379   -332   -327   -734       N  
ATOM   3598  CA  TYR B 136     -19.010  18.155  21.523  1.00 39.41           C  
ANISOU 3598  CA  TYR B 136     4696   5439   4838   -375   -310   -809       C  
ATOM   3599  C   TYR B 136     -19.829  17.783  20.283  1.00 38.52           C  
ANISOU 3599  C   TYR B 136     4538   5413   4684   -380   -348   -889       C  
ATOM   3600  O   TYR B 136     -19.291  17.234  19.313  1.00 41.35           O  
ANISOU 3600  O   TYR B 136     4907   5796   5009   -380   -351   -931       O  
ATOM   3601  CB  TYR B 136     -19.395  17.302  22.740  1.00 38.48           C  
ANISOU 3601  CB  TYR B 136     4572   5246   4804   -423   -274   -826       C  
ATOM   3602  CG  TYR B 136     -19.435  15.814  22.460  1.00 47.06           C  
ANISOU 3602  CG  TYR B 136     5647   6304   5931   -471   -251   -908       C  
ATOM   3603  CD1 TYR B 136     -18.336  15.163  21.907  1.00 49.99           C  
ANISOU 3603  CD1 TYR B 136     6052   6652   6290   -473   -232   -924       C  
ATOM   3604  CD2 TYR B 136     -20.573  15.060  22.741  1.00 51.93           C  
ANISOU 3604  CD2 TYR B 136     6217   6915   6599   -515   -246   -971       C  
ATOM   3605  CE1 TYR B 136     -18.366  13.808  21.639  1.00 48.23           C  
ANISOU 3605  CE1 TYR B 136     5820   6399   6106   -516   -207  -1000       C  
ATOM   3606  CE2 TYR B 136     -20.614  13.708  22.470  1.00 59.07           C  
ANISOU 3606  CE2 TYR B 136     7110   7788   7546   -562   -220  -1049       C  
ATOM   3607  CZ  TYR B 136     -19.506  13.089  21.920  1.00 54.69           C  
ANISOU 3607  CZ  TYR B 136     6593   7210   6979   -562   -201  -1064       C  
ATOM   3608  OH  TYR B 136     -19.540  11.741  21.654  1.00 65.75           O  
ANISOU 3608  OH  TYR B 136     7983   8574   8425   -607   -171  -1143       O  
ATOM   3609  N   VAL B 137     -21.118  18.132  20.272  1.00 34.69           N  
ANISOU 3609  N   VAL B 137     4002   4982   4198   -380   -380   -910       N  
ATOM   3610  CA  VAL B 137     -21.970  17.835  19.121  1.00 39.24           C  
ANISOU 3610  CA  VAL B 137     4528   5651   4732   -382   -422   -988       C  
ATOM   3611  C   VAL B 137     -21.451  18.530  17.863  1.00 47.58           C  
ANISOU 3611  C   VAL B 137     5598   6786   5692   -327   -454   -969       C  
ATOM   3612  O   VAL B 137     -21.401  17.932  16.783  1.00 53.54           O  
ANISOU 3612  O   VAL B 137     6342   7594   6407   -331   -472  -1036       O  
ATOM   3613  CB  VAL B 137     -23.430  18.231  19.417  1.00 42.45           C  
ANISOU 3613  CB  VAL B 137     4873   6102   5154   -386   -451  -1004       C  
ATOM   3614  CG1 VAL B 137     -24.304  18.057  18.164  1.00 44.26           C  
ANISOU 3614  CG1 VAL B 137     5045   6442   5329   -380   -504  -1082       C  
ATOM   3615  CG2 VAL B 137     -23.984  17.403  20.559  1.00 42.39           C  
ANISOU 3615  CG2 VAL B 137     4847   6019   5241   -444   -415  -1033       C  
ATOM   3616  N   VAL B 138     -21.070  19.802  17.978  1.00 40.75           N  
ANISOU 3616  N   VAL B 138     4761   5930   4792   -274   -458   -878       N  
ATOM   3617  CA  VAL B 138     -20.684  20.586  16.806  1.00 41.63           C  
ANISOU 3617  CA  VAL B 138     4885   6120   4814   -215   -484   -848       C  
ATOM   3618  C   VAL B 138     -19.351  20.105  16.236  1.00 52.03           C  
ANISOU 3618  C   VAL B 138     6250   7411   6108   -213   -459   -851       C  
ATOM   3619  O   VAL B 138     -19.209  19.915  15.023  1.00 56.08           O  
ANISOU 3619  O   VAL B 138     6760   7995   6554   -192   -480   -888       O  
ATOM   3620  CB  VAL B 138     -20.636  22.083  17.161  1.00 41.88           C  
ANISOU 3620  CB  VAL B 138     4932   6155   4825   -161   -486   -747       C  
ATOM   3621  CG1 VAL B 138     -19.889  22.867  16.087  1.00 56.41           C  
ANISOU 3621  CG1 VAL B 138     6801   8048   6584   -100   -494   -700       C  
ATOM   3622  CG2 VAL B 138     -22.042  22.610  17.300  1.00 40.69           C  
ANISOU 3622  CG2 VAL B 138     4726   6061   4674   -149   -521   -753       C  
ATOM   3623  N   VAL B 139     -18.350  19.923  17.091  1.00 44.95           N  
ANISOU 3623  N   VAL B 139     5398   6419   5262   -230   -415   -810       N  
ATOM   3624  CA  VAL B 139     -17.016  19.630  16.581  1.00 48.67           C  
ANISOU 3624  CA  VAL B 139     5915   6865   5711   -221   -389   -799       C  
ATOM   3625  C   VAL B 139     -16.861  18.147  16.274  1.00 57.39           C  
ANISOU 3625  C   VAL B 139     7016   7949   6841   -268   -375   -889       C  
ATOM   3626  O   VAL B 139     -16.286  17.775  15.245  1.00 68.08           O  
ANISOU 3626  O   VAL B 139     8384   9337   8147   -256   -375   -920       O  
ATOM   3627  CB  VAL B 139     -15.949  20.127  17.569  1.00 49.76           C  
ANISOU 3627  CB  VAL B 139     6101   6917   5890   -214   -350   -716       C  
ATOM   3628  CG1 VAL B 139     -14.550  19.806  17.054  1.00 56.24           C  
ANISOU 3628  CG1 VAL B 139     6965   7712   6693   -204   -322   -705       C  
ATOM   3629  CG2 VAL B 139     -16.105  21.621  17.789  1.00 49.90           C  
ANISOU 3629  CG2 VAL B 139     6121   6954   5884   -167   -362   -634       C  
ATOM   3630  N   CYS B 140     -17.363  17.278  17.146  1.00 54.89           N  
ANISOU 3630  N   CYS B 140     6680   7574   6599   -322   -357   -931       N  
ATOM   3631  CA  CYS B 140     -17.224  15.842  16.953  1.00 50.80           C  
ANISOU 3631  CA  CYS B 140     6160   7024   6118   -370   -335  -1015       C  
ATOM   3632  C   CYS B 140     -18.320  15.244  16.094  1.00 63.62           C  
ANISOU 3632  C   CYS B 140     7729   8722   7721   -392   -370  -1116       C  
ATOM   3633  O   CYS B 140     -18.200  14.077  15.708  1.00 69.47           O  
ANISOU 3633  O   CYS B 140     8466   9446   8483   -430   -354  -1197       O  
ATOM   3634  CB  CYS B 140     -17.197  15.123  18.303  1.00 50.54           C  
ANISOU 3634  CB  CYS B 140     6134   6888   6182   -416   -291  -1010       C  
ATOM   3635  SG  CYS B 140     -15.705  15.475  19.237  1.00 54.11           S  
ANISOU 3635  SG  CYS B 140     6650   7250   6660   -397   -247   -912       S  
ATOM   3636  N  ALYS B 141     -19.364  16.013  15.784  0.59 60.45           N  
ANISOU 3636  N  ALYS B 141     7286   8404   7280   -369   -417  -1116       N  
ATOM   3637  N  BLYS B 141     -19.365  16.011  15.782  0.41 60.53           N  
ANISOU 3637  N  BLYS B 141     7295   8413   7289   -369   -417  -1117       N  
ATOM   3638  CA ALYS B 141     -20.490  15.610  14.944  0.59 63.78           C  
ANISOU 3638  CA ALYS B 141     7648   8913   7672   -383   -460  -1211       C  
ATOM   3639  CA BLYS B 141     -20.487  15.605  14.938  0.41 63.80           C  
ANISOU 3639  CA BLYS B 141     7651   8916   7675   -383   -460  -1211       C  
ATOM   3640  C  ALYS B 141     -20.904  14.155  15.206  0.59 69.02           C  
ANISOU 3640  C  ALYS B 141     8284   9528   8413   -456   -436  -1311       C  
ATOM   3641  C  BLYS B 141     -20.908  14.152  15.204  0.41 69.01           C  
ANISOU 3641  C  BLYS B 141     8283   9526   8411   -456   -436  -1312       C  
ATOM   3642  O  ALYS B 141     -20.876  13.329  14.293  0.59 74.52           O  
ANISOU 3642  O  ALYS B 141     8969  10259   9088   -475   -444  -1400       O  
ATOM   3643  O  BLYS B 141     -20.892  13.325  14.291  0.41 74.45           O  
ANISOU 3643  O  BLYS B 141     8959  10250   9079   -475   -444  -1401       O  
ATOM   3644  CB ALYS B 141     -20.172  15.831  13.469  0.59 66.49           C  
ANISOU 3644  CB ALYS B 141     7996   9354   7914   -340   -493  -1235       C  
ATOM   3645  CB BLYS B 141     -20.159  15.817  13.464  0.41 66.51           C  
ANISOU 3645  CB BLYS B 141     7998   9356   7916   -340   -493  -1236       C  
ATOM   3646  CG ALYS B 141     -19.882  17.287  13.129  0.59 68.56           C  
ANISOU 3646  CG ALYS B 141     8279   9670   8100   -265   -514  -1136       C  
ATOM   3647  CG BLYS B 141     -19.519  17.169  13.174  0.41 68.19           C  
ANISOU 3647  CG BLYS B 141     8248   9601   8059   -268   -501  -1130       C  
ATOM   3648  CD ALYS B 141     -19.292  17.454  11.737  0.59 72.41           C  
ANISOU 3648  CD ALYS B 141     8786  10238   8489   -219   -532  -1146       C  
ATOM   3649  CD BLYS B 141     -19.320  17.406  11.685  0.41 72.39           C  
ANISOU 3649  CD BLYS B 141     8782  10239   8485   -220   -533  -1152       C  
ATOM   3650  CE ALYS B 141     -18.887  18.904  11.487  0.59 72.19           C  
ANISOU 3650  CE ALYS B 141     8786  10246   8398   -145   -539  -1036       C  
ATOM   3651  CE BLYS B 141     -18.468  18.646  11.433  0.41 72.46           C  
ANISOU 3651  CE BLYS B 141     8836  10260   8436   -151   -525  -1041       C  
ATOM   3652  NZ ALYS B 141     -18.238  19.091  10.160  0.59 73.37           N  
ANISOU 3652  NZ ALYS B 141     8958  10468   8450    -95   -548  -1035       N  
ATOM   3653  NZ BLYS B 141     -18.998  19.857  12.122  0.41 68.56           N  
ANISOU 3653  NZ BLYS B 141     8332   9767   7953   -120   -536   -957       N  
ATOM   3654  N   PRO B 142     -21.288  13.819  16.451  1.00 70.37           N  
ANISOU 3654  N   PRO B 142     8448   9616   8675   -496   -404  -1300       N  
ATOM   3655  CA  PRO B 142     -21.599  12.431  16.798  1.00 68.13           C  
ANISOU 3655  CA  PRO B 142     8143   9269   8474   -564   -369  -1384       C  
ATOM   3656  C   PRO B 142     -23.046  12.057  16.499  1.00 68.70           C  
ANISOU 3656  C   PRO B 142     8138   9401   8564   -600   -402  -1478       C  
ATOM   3657  O   PRO B 142     -23.276  11.155  15.695  1.00 79.89           O  
ANISOU 3657  O   PRO B 142     9527  10847   9979   -632   -410  -1582       O  
ATOM   3658  CB  PRO B 142     -21.327  12.395  18.300  1.00 64.50           C  
ANISOU 3658  CB  PRO B 142     7712   8699   8096   -581   -318  -1313       C  
ATOM   3659  CG  PRO B 142     -21.734  13.753  18.755  1.00 59.56           C  
ANISOU 3659  CG  PRO B 142     7080   8109   7440   -538   -347  -1230       C  
ATOM   3660  CD  PRO B 142     -21.481  14.708  17.610  1.00 65.91           C  
ANISOU 3660  CD  PRO B 142     7891   9012   8140   -480   -395  -1208       C  
ATOM   3661  N   ARG B 147     -28.003  18.140  15.023  1.00 79.52           N  
ANISOU 3661  N   ARG B 147     9278  11295   9639   -346   -695  -1312       N  
ATOM   3662  CA  ARG B 147     -27.462  19.497  15.002  1.00 77.52           C  
ANISOU 3662  CA  ARG B 147     9070  11057   9328   -272   -698  -1195       C  
ATOM   3663  C   ARG B 147     -27.980  20.320  16.185  1.00 71.05           C  
ANISOU 3663  C   ARG B 147     8245  10191   8561   -263   -682  -1119       C  
ATOM   3664  O   ARG B 147     -29.161  20.254  16.518  1.00 79.39           O  
ANISOU 3664  O   ARG B 147     9238  11272   9653   -283   -700  -1154       O  
ATOM   3665  CB  ARG B 147     -27.815  20.187  13.685  1.00 72.27           C  
ANISOU 3665  CB  ARG B 147     8377  10529   8553   -206   -758  -1198       C  
ATOM   3666  CG  ARG B 147     -27.241  21.587  13.543  1.00 71.80           C  
ANISOU 3666  CG  ARG B 147     8364  10486   8432   -126   -757  -1077       C  
ATOM   3667  N   PHE B 148     -27.094  21.092  16.813  1.00 54.12           N  
ANISOU 3667  N   PHE B 148     6165   7979   6422   -234   -648  -1019       N  
ATOM   3668  CA  PHE B 148     -27.442  21.898  17.982  1.00 52.69           C  
ANISOU 3668  CA  PHE B 148     5987   7745   6288   -225   -627   -945       C  
ATOM   3669  C   PHE B 148     -27.858  23.284  17.503  1.00 55.32           C  
ANISOU 3669  C   PHE B 148     6306   8158   6555   -149   -661   -878       C  
ATOM   3670  O   PHE B 148     -27.011  24.092  17.111  1.00 60.12           O  
ANISOU 3670  O   PHE B 148     6963   8771   7110    -97   -656   -807       O  
ATOM   3671  CB  PHE B 148     -26.260  21.980  18.946  1.00 50.36           C  
ANISOU 3671  CB  PHE B 148     5765   7335   6036   -236   -571   -878       C  
ATOM   3672  CG  PHE B 148     -26.636  22.315  20.371  1.00 50.48           C  
ANISOU 3672  CG  PHE B 148     5781   7276   6122   -253   -540   -833       C  
ATOM   3673  CD1 PHE B 148     -26.987  23.610  20.737  1.00 48.21           C  
ANISOU 3673  CD1 PHE B 148     5492   7002   5821   -204   -547   -758       C  
ATOM   3674  CD2 PHE B 148     -26.584  21.341  21.357  1.00 46.14           C  
ANISOU 3674  CD2 PHE B 148     5238   6639   5653   -314   -500   -864       C  
ATOM   3675  CE1 PHE B 148     -27.309  23.914  22.063  1.00 40.66           C  
ANISOU 3675  CE1 PHE B 148     4541   5979   4930   -219   -516   -719       C  
ATOM   3676  CE2 PHE B 148     -26.895  21.638  22.674  1.00 45.20           C  
ANISOU 3676  CE2 PHE B 148     5124   6455   5594   -326   -469   -821       C  
ATOM   3677  CZ  PHE B 148     -27.264  22.927  23.030  1.00 46.73           C  
ANISOU 3677  CZ  PHE B 148     5316   6667   5772   -279   -478   -751       C  
ATOM   3678  N   GLY B 149     -29.164  23.560  17.546  1.00 54.11           N  
ANISOU 3678  N   GLY B 149     6087   8066   6408   -141   -693   -898       N  
ATOM   3679  CA  GLY B 149     -29.720  24.794  17.058  1.00 55.51           C  
ANISOU 3679  CA  GLY B 149     6241   8326   6525    -68   -728   -841       C  
ATOM   3680  C   GLY B 149     -30.239  25.685  18.167  1.00 43.90           C  
ANISOU 3680  C   GLY B 149     4766   6809   5104    -54   -707   -772       C  
ATOM   3681  O   GLY B 149     -29.889  25.529  19.344  1.00 44.00           O  
ANISOU 3681  O   GLY B 149     4811   6718   5187    -91   -660   -749       O  
ATOM   3682  N   GLU B 150     -31.084  26.646  17.779  1.00 47.40           N  
ANISOU 3682  N   GLU B 150     5169   7334   5507      6   -740   -738       N  
ATOM   3683  CA  GLU B 150     -31.630  27.609  18.734  1.00 49.86           C  
ANISOU 3683  CA  GLU B 150     5474   7611   5859     28   -722   -669       C  
ATOM   3684  C   GLU B 150     -32.514  26.926  19.768  1.00 45.35           C  
ANISOU 3684  C   GLU B 150     4860   6995   5376    -35   -708   -721       C  
ATOM   3685  O   GLU B 150     -32.465  27.271  20.958  1.00 37.74           O  
ANISOU 3685  O   GLU B 150     3921   5947   4472    -48   -666   -674       O  
ATOM   3686  CB  GLU B 150     -32.422  28.697  17.998  1.00 51.40           C  
ANISOU 3686  CB  GLU B 150     5628   7911   5991    108   -762   -627       C  
ATOM   3687  CG  GLU B 150     -31.673  30.013  17.828  1.00 56.17           C  
ANISOU 3687  CG  GLU B 150     6290   8501   6552    181   -742   -518       C  
ATOM   3688  CD  GLU B 150     -32.427  31.037  16.993  1.00 53.55           C  
ANISOU 3688  CD  GLU B 150     5919   8277   6153    266   -780   -474       C  
ATOM   3689  OE1 GLU B 150     -32.460  30.893  15.750  1.00 66.52           O  
ANISOU 3689  OE1 GLU B 150     7542  10020   7714    302   -822   -499       O  
ATOM   3690  OE2 GLU B 150     -32.982  31.990  17.576  1.00 51.06           O  
ANISOU 3690  OE2 GLU B 150     5592   7947   5863    301   -767   -413       O  
ATOM   3691  N   ASN B 151     -33.341  25.970  19.324  1.00 39.47           N  
ANISOU 3691  N   ASN B 151     4048   6308   4639    -74   -740   -818       N  
ATOM   3692  CA  ASN B 151     -34.245  25.257  20.225  1.00 40.44           C  
ANISOU 3692  CA  ASN B 151     4122   6393   4849   -136   -724   -872       C  
ATOM   3693  C   ASN B 151     -33.467  24.583  21.340  1.00 40.42           C  
ANISOU 3693  C   ASN B 151     4176   6262   4920   -195   -663   -867       C  
ATOM   3694  O   ASN B 151     -33.836  24.665  22.515  1.00 40.76           O  
ANISOU 3694  O   ASN B 151     4218   6237   5031   -218   -627   -843       O  
ATOM   3695  CB  ASN B 151     -35.055  24.209  19.447  1.00 40.76           C  
ANISOU 3695  CB  ASN B 151     4087   6512   4889   -175   -766   -988       C  
ATOM   3696  CG  ASN B 151     -36.141  24.824  18.601  1.00 51.13           C  
ANISOU 3696  CG  ASN B 151     5325   7957   6147   -122   -828  -1000       C  
ATOM   3697  OD1 ASN B 151     -36.546  25.963  18.831  1.00 53.64           O  
ANISOU 3697  OD1 ASN B 151     5636   8296   6450    -65   -832   -924       O  
ATOM   3698  ND2 ASN B 151     -36.633  24.068  17.616  1.00 41.31           N  
ANISOU 3698  ND2 ASN B 151     4020   6803   4871   -141   -876  -1098       N  
ATOM   3699  N   HIS B 152     -32.367  23.918  20.982  1.00 36.51           N  
ANISOU 3699  N   HIS B 152     3732   5732   4409   -217   -649   -886       N  
ATOM   3700  CA  HIS B 152     -31.560  23.262  21.997  1.00 39.20           C  
ANISOU 3700  CA  HIS B 152     4126   5954   4813   -267   -592   -878       C  
ATOM   3701  C   HIS B 152     -30.888  24.274  22.907  1.00 36.18           C  
ANISOU 3701  C   HIS B 152     3806   5502   4438   -234   -557   -776       C  
ATOM   3702  O   HIS B 152     -30.720  24.001  24.101  1.00 32.85           O  
ANISOU 3702  O   HIS B 152     3409   4991   4081   -268   -512   -759       O  
ATOM   3703  CB  HIS B 152     -30.528  22.353  21.337  1.00 41.46           C  
ANISOU 3703  CB  HIS B 152     4450   6225   5078   -292   -587   -921       C  
ATOM   3704  CG  HIS B 152     -31.118  21.494  20.270  1.00 44.11           C  
ANISOU 3704  CG  HIS B 152     4727   6640   5392   -316   -627  -1023       C  
ATOM   3705  ND1 HIS B 152     -31.068  21.832  18.937  1.00 52.67           N  
ANISOU 3705  ND1 HIS B 152     5797   7828   6386   -270   -677  -1038       N  
ATOM   3706  CD2 HIS B 152     -31.839  20.351  20.347  1.00 51.92           C  
ANISOU 3706  CD2 HIS B 152     5663   7625   6438   -380   -624  -1118       C  
ATOM   3707  CE1 HIS B 152     -31.705  20.916  18.232  1.00 59.20           C  
ANISOU 3707  CE1 HIS B 152     6566   8715   7213   -306   -708  -1142       C  
ATOM   3708  NE2 HIS B 152     -32.182  20.007  19.064  1.00 55.32           N  
ANISOU 3708  NE2 HIS B 152     6049   8157   6814   -374   -676  -1194       N  
ATOM   3709  N   ALA B 153     -30.493  25.430  22.372  1.00 35.29           N  
ANISOU 3709  N   ALA B 153     3718   5429   4261   -168   -575   -709       N  
ATOM   3710  CA  ALA B 153     -29.860  26.435  23.224  1.00 36.64           C  
ANISOU 3710  CA  ALA B 153     3945   5533   4443   -138   -540   -618       C  
ATOM   3711  C   ALA B 153     -30.837  26.940  24.270  1.00 29.78           C  
ANISOU 3711  C   ALA B 153     3047   4643   3626   -138   -526   -594       C  
ATOM   3712  O   ALA B 153     -30.508  27.020  25.451  1.00 28.32           O  
ANISOU 3712  O   ALA B 153     2898   4372   3490   -158   -483   -560       O  
ATOM   3713  CB  ALA B 153     -29.339  27.601  22.388  1.00 33.77           C  
ANISOU 3713  CB  ALA B 153     3608   5217   4006    -67   -559   -552       C  
ATOM   3714  N   ILE B 154     -32.054  27.282  23.843  1.00 32.99           N  
ANISOU 3714  N   ILE B 154     3386   5129   4018   -115   -561   -611       N  
ATOM   3715  CA  ILE B 154     -33.060  27.791  24.771  1.00 35.02           C  
ANISOU 3715  CA  ILE B 154     3611   5372   4324   -111   -548   -589       C  
ATOM   3716  C   ILE B 154     -33.427  26.729  25.798  1.00 34.31           C  
ANISOU 3716  C   ILE B 154     3506   5216   4314   -182   -513   -638       C  
ATOM   3717  O   ILE B 154     -33.576  27.017  26.999  1.00 29.28           O  
ANISOU 3717  O   ILE B 154     2885   4513   3726   -191   -474   -602       O  
ATOM   3718  CB  ILE B 154     -34.280  28.279  23.970  1.00 36.97           C  
ANISOU 3718  CB  ILE B 154     3781   5728   4536    -70   -597   -604       C  
ATOM   3719  CG1 ILE B 154     -33.848  29.456  23.086  1.00 37.26           C  
ANISOU 3719  CG1 ILE B 154     3843   5820   4496      9   -620   -536       C  
ATOM   3720  CG2 ILE B 154     -35.470  28.606  24.890  1.00 35.46           C  
ANISOU 3720  CG2 ILE B 154     3543   5528   4403    -74   -583   -596       C  
ATOM   3721  CD1 ILE B 154     -34.865  29.853  22.047  1.00 42.88           C  
ANISOU 3721  CD1 ILE B 154     4484   6654   5155     58   -674   -551       C  
ATOM   3722  N   MET B 155     -33.558  25.481  25.351  1.00 31.13           N  
ANISOU 3722  N   MET B 155     3075   4828   3926   -233   -523   -720       N  
ATOM   3723  CA  MET B 155     -33.805  24.390  26.284  1.00 32.62           C  
ANISOU 3723  CA  MET B 155     3254   4945   4194   -301   -482   -765       C  
ATOM   3724  C   MET B 155     -32.672  24.285  27.297  1.00 31.44           C  
ANISOU 3724  C   MET B 155     3185   4690   4072   -316   -430   -716       C  
ATOM   3725  O   MET B 155     -32.913  24.094  28.493  1.00 31.80           O  
ANISOU 3725  O   MET B 155     3238   4669   4177   -341   -387   -702       O  
ATOM   3726  CB  MET B 155     -33.976  23.085  25.503  1.00 38.24           C  
ANISOU 3726  CB  MET B 155     3927   5686   4915   -351   -500   -863       C  
ATOM   3727  CG  MET B 155     -34.103  21.844  26.347  1.00 47.95           C  
ANISOU 3727  CG  MET B 155     5152   6836   6229   -422   -452   -911       C  
ATOM   3728  SD  MET B 155     -35.194  20.668  25.521  1.00 61.95           S  
ANISOU 3728  SD  MET B 155     6832   8673   8033   -476   -481  -1036       S  
ATOM   3729  CE  MET B 155     -34.710  20.932  23.812  1.00 40.69           C  
ANISOU 3729  CE  MET B 155     4138   6087   5236   -434   -548  -1062       C  
ATOM   3730  N   GLY B 156     -31.431  24.448  26.835  1.00 27.63           N  
ANISOU 3730  N   GLY B 156     2761   4194   3542   -296   -432   -688       N  
ATOM   3731  CA  GLY B 156     -30.305  24.452  27.751  1.00 26.38           C  
ANISOU 3731  CA  GLY B 156     2676   3945   3403   -304   -388   -640       C  
ATOM   3732  C   GLY B 156     -30.390  25.578  28.763  1.00 26.41           C  
ANISOU 3732  C   GLY B 156     2703   3914   3418   -271   -367   -566       C  
ATOM   3733  O   GLY B 156     -30.043  25.395  29.928  1.00 27.77           O  
ANISOU 3733  O   GLY B 156     2909   4010   3631   -292   -324   -543       O  
ATOM   3734  N   VAL B 157     -30.833  26.765  28.321  1.00 30.26           N  
ANISOU 3734  N   VAL B 157     3172   4458   3867   -218   -394   -529       N  
ATOM   3735  CA  VAL B 157     -30.989  27.897  29.240  1.00 27.38           C  
ANISOU 3735  CA  VAL B 157     2826   4063   3516   -186   -373   -463       C  
ATOM   3736  C   VAL B 157     -31.968  27.543  30.355  1.00 28.06           C  
ANISOU 3736  C   VAL B 157     2881   4116   3666   -217   -344   -480       C  
ATOM   3737  O   VAL B 157     -31.682  27.751  31.544  1.00 24.65           O  
ANISOU 3737  O   VAL B 157     2485   3615   3264   -223   -304   -445       O  
ATOM   3738  CB  VAL B 157     -31.450  29.165  28.489  1.00 29.76           C  
ANISOU 3738  CB  VAL B 157     3104   4434   3769   -121   -406   -424       C  
ATOM   3739  CG1 VAL B 157     -31.874  30.267  29.506  1.00 33.08           C  
ANISOU 3739  CG1 VAL B 157     3532   4822   4216    -92   -380   -367       C  
ATOM   3740  CG2 VAL B 157     -30.365  29.686  27.534  1.00 31.00           C  
ANISOU 3740  CG2 VAL B 157     3303   4611   3865    -83   -422   -391       C  
ATOM   3741  N   ALA B 158     -33.148  27.017  29.990  1.00 26.31           N  
ANISOU 3741  N   ALA B 158     2588   3946   3464   -236   -364   -534       N  
ATOM   3742  CA  ALA B 158     -34.139  26.667  31.011  1.00 30.50           C  
ANISOU 3742  CA  ALA B 158     3083   4446   4060   -267   -332   -551       C  
ATOM   3743  C   ALA B 158     -33.580  25.616  31.964  1.00 25.63           C  
ANISOU 3743  C   ALA B 158     2505   3744   3492   -319   -283   -565       C  
ATOM   3744  O   ALA B 158     -33.776  25.689  33.181  1.00 27.06           O  
ANISOU 3744  O   ALA B 158     2701   3868   3713   -328   -240   -538       O  
ATOM   3745  CB  ALA B 158     -35.421  26.155  30.350  1.00 32.20           C  
ANISOU 3745  CB  ALA B 158     3210   4733   4291   -285   -363   -617       C  
ATOM   3746  N   PHE B 159     -32.863  24.639  31.416  1.00 25.75           N  
ANISOU 3746  N   PHE B 159     2536   3748   3500   -350   -287   -604       N  
ATOM   3747  CA  PHE B 159     -32.231  23.603  32.225  1.00 23.74           C  
ANISOU 3747  CA  PHE B 159     2320   3411   3288   -395   -239   -614       C  
ATOM   3748  C   PHE B 159     -31.295  24.198  33.270  1.00 27.22           C  
ANISOU 3748  C   PHE B 159     2832   3787   3723   -373   -206   -544       C  
ATOM   3749  O   PHE B 159     -31.234  23.700  34.401  1.00 24.06           O  
ANISOU 3749  O   PHE B 159     2454   3323   3366   -397   -160   -533       O  
ATOM   3750  CB  PHE B 159     -31.469  22.655  31.296  1.00 28.93           C  
ANISOU 3750  CB  PHE B 159     2989   4073   3928   -420   -253   -660       C  
ATOM   3751  CG  PHE B 159     -30.555  21.671  32.001  1.00 29.33           C  
ANISOU 3751  CG  PHE B 159     3091   4040   4013   -455   -205   -659       C  
ATOM   3752  CD1 PHE B 159     -31.071  20.525  32.585  1.00 34.22           C  
ANISOU 3752  CD1 PHE B 159     3688   4614   4700   -505   -164   -699       C  
ATOM   3753  CD2 PHE B 159     -29.182  21.854  32.001  1.00 34.06           C  
ANISOU 3753  CD2 PHE B 159     3756   4608   4577   -436   -201   -620       C  
ATOM   3754  CE1 PHE B 159     -30.243  19.608  33.211  1.00 35.45           C  
ANISOU 3754  CE1 PHE B 159     3890   4694   4886   -531   -118   -694       C  
ATOM   3755  CE2 PHE B 159     -28.335  20.932  32.619  1.00 38.44           C  
ANISOU 3755  CE2 PHE B 159     4355   5090   5161   -464   -159   -617       C  
ATOM   3756  CZ  PHE B 159     -28.873  19.809  33.234  1.00 29.95           C  
ANISOU 3756  CZ  PHE B 159     3260   3970   4151   -509   -117   -652       C  
ATOM   3757  N   THR B 160     -30.511  25.227  32.904  1.00 23.19           N  
ANISOU 3757  N   THR B 160     2360   3293   3159   -329   -229   -497       N  
ATOM   3758  CA  THR B 160     -29.564  25.772  33.886  1.00 21.40           C  
ANISOU 3758  CA  THR B 160     2198   3006   2927   -312   -200   -439       C  
ATOM   3759  C   THR B 160     -30.293  26.398  35.069  1.00 21.34           C  
ANISOU 3759  C   THR B 160     2186   2975   2949   -301   -172   -408       C  
ATOM   3760  O   THR B 160     -29.800  26.338  36.204  1.00 24.02           O  
ANISOU 3760  O   THR B 160     2567   3254   3305   -307   -134   -381       O  
ATOM   3761  CB  THR B 160     -28.603  26.795  33.253  1.00 22.92           C  
ANISOU 3761  CB  THR B 160     2428   3217   3064   -268   -225   -398       C  
ATOM   3762  OG1 THR B 160     -29.308  27.981  32.854  1.00 25.59           O  
ANISOU 3762  OG1 THR B 160     2738   3606   3379   -225   -250   -373       O  
ATOM   3763  CG2 THR B 160     -27.853  26.181  32.068  1.00 21.20           C  
ANISOU 3763  CG2 THR B 160     2217   3023   2814   -277   -250   -427       C  
ATOM   3764  N   TRP B 161     -31.453  27.023  34.827  1.00 24.52           N  
ANISOU 3764  N   TRP B 161     2535   3426   3354   -282   -189   -411       N  
ATOM   3765  CA  TRP B 161     -32.215  27.601  35.934  1.00 25.33           C  
ANISOU 3765  CA  TRP B 161     2630   3507   3487   -271   -160   -384       C  
ATOM   3766  C   TRP B 161     -32.801  26.514  36.822  1.00 25.86           C  
ANISOU 3766  C   TRP B 161     2680   3534   3612   -316   -118   -413       C  
ATOM   3767  O   TRP B 161     -32.787  26.637  38.050  1.00 22.09           O  
ANISOU 3767  O   TRP B 161     2230   3008   3156   -316    -77   -384       O  
ATOM   3768  CB  TRP B 161     -33.324  28.513  35.402  1.00 22.16           C  
ANISOU 3768  CB  TRP B 161     2173   3170   3076   -236   -188   -380       C  
ATOM   3769  CG  TRP B 161     -32.802  29.833  34.996  1.00 24.57           C  
ANISOU 3769  CG  TRP B 161     2506   3493   3335   -183   -209   -331       C  
ATOM   3770  CD1 TRP B 161     -32.260  30.178  33.788  1.00 29.66           C  
ANISOU 3770  CD1 TRP B 161     3156   4181   3931   -157   -247   -325       C  
ATOM   3771  CD2 TRP B 161     -32.724  30.993  35.825  1.00 22.83           C  
ANISOU 3771  CD2 TRP B 161     2316   3242   3115   -149   -187   -279       C  
ATOM   3772  NE1 TRP B 161     -31.860  31.500  33.814  1.00 31.14           N  
ANISOU 3772  NE1 TRP B 161     3374   4364   4093   -109   -247   -270       N  
ATOM   3773  CE2 TRP B 161     -32.129  32.018  35.055  1.00 30.56           C  
ANISOU 3773  CE2 TRP B 161     3317   4245   4051   -104   -211   -243       C  
ATOM   3774  CE3 TRP B 161     -33.102  31.266  37.146  1.00 29.65           C  
ANISOU 3774  CE3 TRP B 161     3191   4061   4012   -151   -146   -260       C  
ATOM   3775  CZ2 TRP B 161     -31.913  33.303  35.559  1.00 27.81           C  
ANISOU 3775  CZ2 TRP B 161     2999   3872   3697    -65   -195   -193       C  
ATOM   3776  CZ3 TRP B 161     -32.881  32.551  37.650  1.00 28.48           C  
ANISOU 3776  CZ3 TRP B 161     3075   3894   3854   -111   -133   -213       C  
ATOM   3777  CH2 TRP B 161     -32.294  33.547  36.860  1.00 30.66           C  
ANISOU 3777  CH2 TRP B 161     3369   4188   4091    -70   -157   -182       C  
ATOM   3778  N   VAL B 162     -33.325  25.443  36.223  1.00 25.66           N  
ANISOU 3778  N   VAL B 162     2608   3529   3612   -354   -125   -470       N  
ATOM   3779  CA  VAL B 162     -33.879  24.354  37.030  1.00 26.64           C  
ANISOU 3779  CA  VAL B 162     2714   3609   3799   -400    -78   -498       C  
ATOM   3780  C   VAL B 162     -32.788  23.735  37.905  1.00 29.21           C  
ANISOU 3780  C   VAL B 162     3107   3859   4132   -415    -36   -474       C  
ATOM   3781  O   VAL B 162     -32.968  23.542  39.107  1.00 23.58           O  
ANISOU 3781  O   VAL B 162     2412   3098   3450   -422     13   -452       O  
ATOM   3782  CB  VAL B 162     -34.538  23.295  36.128  1.00 26.89           C  
ANISOU 3782  CB  VAL B 162     2684   3674   3861   -442    -94   -571       C  
ATOM   3783  CG1 VAL B 162     -34.982  22.106  36.965  1.00 29.00           C  
ANISOU 3783  CG1 VAL B 162     2938   3883   4199   -491    -36   -597       C  
ATOM   3784  CG2 VAL B 162     -35.723  23.883  35.369  1.00 26.86           C  
ANISOU 3784  CG2 VAL B 162     2605   3750   3851   -425   -136   -596       C  
ATOM   3785  N   MET B 163     -31.635  23.414  37.319  1.00 21.88           N  
ANISOU 3785  N   MET B 163     2217   2923   3172   -417    -52   -477       N  
ATOM   3786  CA  MET B 163     -30.576  22.802  38.132  1.00 23.87           C  
ANISOU 3786  CA  MET B 163     2530   3108   3430   -428    -14   -453       C  
ATOM   3787  C   MET B 163     -30.056  23.761  39.197  1.00 25.53           C  
ANISOU 3787  C   MET B 163     2791   3292   3618   -392      2   -392       C  
ATOM   3788  O   MET B 163     -29.798  23.353  40.342  1.00 24.05           O  
ANISOU 3788  O   MET B 163     2636   3052   3449   -399     47   -369       O  
ATOM   3789  CB  MET B 163     -29.421  22.331  37.248  1.00 27.38           C  
ANISOU 3789  CB  MET B 163     3004   3553   3845   -434    -36   -468       C  
ATOM   3790  CG  MET B 163     -29.803  21.264  36.264  1.00 28.59           C  
ANISOU 3790  CG  MET B 163     3114   3726   4022   -472    -47   -534       C  
ATOM   3791  SD  MET B 163     -30.578  19.814  37.031  1.00 32.66           S  
ANISOU 3791  SD  MET B 163     3602   4186   4621   -526     15   -570       S  
ATOM   3792  CE  MET B 163     -29.345  19.302  38.211  1.00 36.26           C  
ANISOU 3792  CE  MET B 163     4136   4560   5083   -522     68   -519       C  
ATOM   3793  N   ALA B 164     -29.858  25.032  38.841  1.00 24.70           N  
ANISOU 3793  N   ALA B 164     2694   3220   3470   -353    -33   -365       N  
ATOM   3794  CA  ALA B 164     -29.333  25.979  39.816  1.00 21.34           C  
ANISOU 3794  CA  ALA B 164     2316   2769   3025   -322    -18   -315       C  
ATOM   3795  C   ALA B 164     -30.305  26.169  40.973  1.00 23.27           C  
ANISOU 3795  C   ALA B 164     2545   2995   3300   -320     19   -302       C  
ATOM   3796  O   ALA B 164     -29.892  26.251  42.137  1.00 23.21           O  
ANISOU 3796  O   ALA B 164     2580   2947   3292   -313     52   -273       O  
ATOM   3797  CB  ALA B 164     -29.039  27.319  39.147  1.00 22.20           C  
ANISOU 3797  CB  ALA B 164     2430   2914   3091   -282    -58   -292       C  
ATOM   3798  N   LEU B 165     -31.599  26.249  40.668  1.00 22.07           N  
ANISOU 3798  N   LEU B 165     2335   2878   3175   -325     15   -325       N  
ATOM   3799  CA  LEU B 165     -32.607  26.359  41.723  1.00 21.25           C  
ANISOU 3799  CA  LEU B 165     2211   2757   3105   -325     54   -315       C  
ATOM   3800  C   LEU B 165     -32.643  25.105  42.583  1.00 24.81           C  
ANISOU 3800  C   LEU B 165     2672   3157   3596   -360    107   -323       C  
ATOM   3801  O   LEU B 165     -32.917  25.178  43.781  1.00 25.48           O  
ANISOU 3801  O   LEU B 165     2775   3211   3696   -354    151   -298       O  
ATOM   3802  CB  LEU B 165     -33.989  26.615  41.111  1.00 21.76           C  
ANISOU 3802  CB  LEU B 165     2201   2872   3193   -325     37   -341       C  
ATOM   3803  CG  LEU B 165     -34.224  28.056  40.616  1.00 23.02           C  
ANISOU 3803  CG  LEU B 165     2350   3077   3319   -279      0   -318       C  
ATOM   3804  CD1 LEU B 165     -35.481  28.140  39.751  1.00 27.50           C  
ANISOU 3804  CD1 LEU B 165     2838   3706   3903   -278    -28   -349       C  
ATOM   3805  CD2 LEU B 165     -34.300  29.029  41.792  1.00 26.24           C  
ANISOU 3805  CD2 LEU B 165     2788   3456   3724   -248     31   -275       C  
ATOM   3806  N   ALA B 166     -32.414  23.941  41.984  1.00 25.10           N  
ANISOU 3806  N   ALA B 166     2698   3186   3653   -396    107   -358       N  
ATOM   3807  CA  ALA B 166     -32.391  22.717  42.771  1.00 21.87           C  
ANISOU 3807  CA  ALA B 166     2302   2723   3286   -427    163   -362       C  
ATOM   3808  C   ALA B 166     -31.215  22.690  43.742  1.00 28.29           C  
ANISOU 3808  C   ALA B 166     3188   3490   4071   -409    188   -317       C  
ATOM   3809  O   ALA B 166     -31.222  21.908  44.695  1.00 25.54           O  
ANISOU 3809  O   ALA B 166     2858   3096   3749   -420    242   -303       O  
ATOM   3810  CB  ALA B 166     -32.350  21.507  41.840  1.00 23.43           C  
ANISOU 3810  CB  ALA B 166     2472   2918   3512   -469    158   -413       C  
ATOM   3811  N   CYS B 167     -30.197  23.516  43.508  1.00 22.20           N  
ANISOU 3811  N   CYS B 167     2456   2732   3246   -379    151   -295       N  
ATOM   3812  CA  CYS B 167     -29.111  23.697  44.461  1.00 24.62           C  
ANISOU 3812  CA  CYS B 167     2827   3006   3522   -357    168   -254       C  
ATOM   3813  C   CYS B 167     -29.390  24.835  45.453  1.00 24.11           C  
ANISOU 3813  C   CYS B 167     2779   2945   3438   -324    178   -222       C  
ATOM   3814  O   CYS B 167     -29.229  24.661  46.667  1.00 26.22           O  
ANISOU 3814  O   CYS B 167     3078   3181   3703   -315    218   -195       O  
ATOM   3815  CB  CYS B 167     -27.797  23.960  43.704  1.00 23.54           C  
ANISOU 3815  CB  CYS B 167     2722   2879   3343   -346    126   -251       C  
ATOM   3816  SG  CYS B 167     -26.377  24.017  44.832  1.00 26.24           S  
ANISOU 3816  SG  CYS B 167     3136   3184   3650   -323    144   -208       S  
ATOM   3817  N   ALA B 168     -29.809  26.000  44.956  1.00 22.70           N  
ANISOU 3817  N   ALA B 168     2579   2803   3244   -304    144   -222       N  
ATOM   3818  CA  ALA B 168     -29.878  27.217  45.768  1.00 20.12           C  
ANISOU 3818  CA  ALA B 168     2272   2477   2894   -269    149   -194       C  
ATOM   3819  C   ALA B 168     -31.141  27.298  46.622  1.00 23.68           C  
ANISOU 3819  C   ALA B 168     2696   2923   3376   -268    190   -190       C  
ATOM   3820  O   ALA B 168     -31.137  27.963  47.669  1.00 21.56           O  
ANISOU 3820  O   ALA B 168     2456   2643   3093   -244    212   -167       O  
ATOM   3821  CB  ALA B 168     -29.803  28.454  44.853  1.00 20.87           C  
ANISOU 3821  CB  ALA B 168     2356   2609   2965   -245    102   -193       C  
ATOM   3822  N   ALA B 169     -32.236  26.676  46.184  1.00 21.12           N  
ANISOU 3822  N   ALA B 169     2317   2612   3096   -292    199   -216       N  
ATOM   3823  CA  ALA B 169     -33.503  26.870  46.884  1.00 21.27           C  
ANISOU 3823  CA  ALA B 169     2303   2631   3147   -289    236   -214       C  
ATOM   3824  C   ALA B 169     -33.708  26.018  48.144  1.00 23.22           C  
ANISOU 3824  C   ALA B 169     2569   2835   3419   -301    301   -199       C  
ATOM   3825  O   ALA B 169     -34.331  26.499  49.098  1.00 23.50           O  
ANISOU 3825  O   ALA B 169     2606   2864   3459   -282    335   -180       O  
ATOM   3826  CB  ALA B 169     -34.676  26.651  45.917  1.00 23.48           C  
ANISOU 3826  CB  ALA B 169     2506   2947   3466   -309    219   -249       C  
ATOM   3827  N   PRO B 170     -33.280  24.758  48.211  1.00 21.54           N  
ANISOU 3827  N   PRO B 170     2369   2591   3224   -328    325   -205       N  
ATOM   3828  CA  PRO B 170     -33.594  23.960  49.419  1.00 24.96           C  
ANISOU 3828  CA  PRO B 170     2818   2984   3684   -335    394   -185       C  
ATOM   3829  C   PRO B 170     -33.137  24.612  50.723  1.00 24.43           C  
ANISOU 3829  C   PRO B 170     2806   2903   3573   -296    418   -144       C  
ATOM   3830  O   PRO B 170     -33.871  24.538  51.721  1.00 25.83           O  
ANISOU 3830  O   PRO B 170     2981   3065   3767   -289    471   -126       O  
ATOM   3831  CB  PRO B 170     -32.886  22.622  49.152  1.00 25.54           C  
ANISOU 3831  CB  PRO B 170     2906   3024   3773   -363    408   -193       C  
ATOM   3832  CG  PRO B 170     -33.003  22.490  47.637  1.00 22.27           C  
ANISOU 3832  CG  PRO B 170     2447   2640   3374   -389    357   -238       C  
ATOM   3833  CD  PRO B 170     -32.671  23.903  47.157  1.00 22.32           C  
ANISOU 3833  CD  PRO B 170     2462   2690   3330   -357    298   -232       C  
ATOM   3834  N   PRO B 171     -31.973  25.292  50.785  1.00 27.63           N  
ANISOU 3834  N   PRO B 171     3260   3317   3922   -271    382   -129       N  
ATOM   3835  CA  PRO B 171     -31.582  25.912  52.067  1.00 22.25           C  
ANISOU 3835  CA  PRO B 171     2628   2627   3198   -235    404    -98       C  
ATOM   3836  C   PRO B 171     -32.472  27.057  52.486  1.00 24.85           C  
ANISOU 3836  C   PRO B 171     2941   2975   3527   -213    411    -96       C  
ATOM   3837  O   PRO B 171     -32.359  27.520  53.630  1.00 22.11           O  
ANISOU 3837  O   PRO B 171     2630   2622   3150   -185    437    -75       O  
ATOM   3838  CB  PRO B 171     -30.132  26.400  51.827  1.00 25.86           C  
ANISOU 3838  CB  PRO B 171     3131   3093   3604   -219    357    -93       C  
ATOM   3839  CG  PRO B 171     -29.635  25.591  50.698  1.00 28.89           C  
ANISOU 3839  CG  PRO B 171     3500   3473   4003   -247    331   -111       C  
ATOM   3840  CD  PRO B 171     -30.859  25.334  49.824  1.00 20.79           C  
ANISOU 3840  CD  PRO B 171     2410   2461   3029   -275    330   -140       C  
ATOM   3841  N   LEU B 172     -33.335  27.555  51.598  1.00 22.24           N  
ANISOU 3841  N   LEU B 172     2558   2670   3225   -221    386   -117       N  
ATOM   3842  CA  LEU B 172     -34.324  28.536  52.020  1.00 25.16           C  
ANISOU 3842  CA  LEU B 172     2905   3052   3601   -199    400   -113       C  
ATOM   3843  C   LEU B 172     -35.476  27.908  52.779  1.00 22.98           C  
ANISOU 3843  C   LEU B 172     2601   2761   3368   -209    463   -108       C  
ATOM   3844  O   LEU B 172     -36.175  28.628  53.500  1.00 26.55           O  
ANISOU 3844  O   LEU B 172     3050   3218   3822   -186    490    -98       O  
ATOM   3845  CB  LEU B 172     -34.907  29.279  50.810  1.00 22.96           C  
ANISOU 3845  CB  LEU B 172     2575   2810   3340   -198    355   -134       C  
ATOM   3846  CG  LEU B 172     -33.952  30.147  49.981  1.00 21.13           C  
ANISOU 3846  CG  LEU B 172     2364   2596   3070   -183    296   -135       C  
ATOM   3847  CD1 LEU B 172     -34.749  30.708  48.787  1.00 29.78           C  
ANISOU 3847  CD1 LEU B 172     3401   3731   4185   -180    260   -151       C  
ATOM   3848  CD2 LEU B 172     -33.385  31.259  50.826  1.00 27.51           C  
ANISOU 3848  CD2 LEU B 172     3220   3395   3838   -148    300   -117       C  
ATOM   3849  N   VAL B 173     -35.721  26.604  52.592  1.00 24.70           N  
ANISOU 3849  N   VAL B 173     2797   2960   3627   -243    489   -117       N  
ATOM   3850  CA  VAL B 173     -36.973  25.998  53.051  1.00 26.03           C  
ANISOU 3850  CA  VAL B 173     2924   3116   3852   -260    548   -118       C  
ATOM   3851  C   VAL B 173     -36.763  24.734  53.885  1.00 31.66           C  
ANISOU 3851  C   VAL B 173     3664   3785   4582   -274    610    -98       C  
ATOM   3852  O   VAL B 173     -37.676  23.912  54.014  1.00 28.75           O  
ANISOU 3852  O   VAL B 173     3255   3396   4272   -300    660   -105       O  
ATOM   3853  CB  VAL B 173     -37.889  25.707  51.840  1.00 26.76           C  
ANISOU 3853  CB  VAL B 173     2937   3231   4000   -293    523   -158       C  
ATOM   3854  CG1 VAL B 173     -38.299  27.023  51.157  1.00 29.96           C  
ANISOU 3854  CG1 VAL B 173     3311   3681   4390   -270    472   -169       C  
ATOM   3855  CG2 VAL B 173     -37.168  24.812  50.844  1.00 23.08           C  
ANISOU 3855  CG2 VAL B 173     2469   2760   3539   -326    491   -182       C  
ATOM   3856  N   GLY B 174     -35.581  24.565  54.476  1.00 22.81           N  
ANISOU 3856  N   GLY B 174     2609   2647   3409   -255    612    -72       N  
ATOM   3857  CA  GLY B 174     -35.418  23.533  55.495  1.00 27.57           C  
ANISOU 3857  CA  GLY B 174     3245   3212   4018   -253    680    -41       C  
ATOM   3858  C   GLY B 174     -34.454  22.423  55.162  1.00 27.90           C  
ANISOU 3858  C   GLY B 174     3311   3227   4061   -271    678    -37       C  
ATOM   3859  O   GLY B 174     -34.314  21.496  55.970  1.00 25.16           O  
ANISOU 3859  O   GLY B 174     2992   2846   3723   -268    738     -7       O  
ATOM   3860  N   TRP B 175     -33.758  22.422  54.034  1.00 24.58           N  
ANISOU 3860  N   TRP B 175     2886   2821   3634   -288    618    -64       N  
ATOM   3861  CA  TRP B 175     -32.746  21.402  53.790  1.00 22.50           C  
ANISOU 3861  CA  TRP B 175     2650   2531   3367   -300    619    -58       C  
ATOM   3862  C   TRP B 175     -31.424  22.157  53.719  1.00 23.46           C  
ANISOU 3862  C   TRP B 175     2820   2675   3417   -271    562    -48       C  
ATOM   3863  O   TRP B 175     -31.189  22.901  52.766  1.00 21.62           O  
ANISOU 3863  O   TRP B 175     2572   2472   3170   -275    500    -74       O  
ATOM   3864  CB  TRP B 175     -33.025  20.607  52.515  1.00 24.80           C  
ANISOU 3864  CB  TRP B 175     2893   2815   3715   -347    602   -100       C  
ATOM   3865  CG  TRP B 175     -32.142  19.407  52.401  1.00 26.90           C  
ANISOU 3865  CG  TRP B 175     3186   3044   3990   -361    622    -92       C  
ATOM   3866  CD1 TRP B 175     -31.499  18.755  53.427  1.00 27.60           C  
ANISOU 3866  CD1 TRP B 175     3328   3099   4062   -338    671    -47       C  
ATOM   3867  CD2 TRP B 175     -31.826  18.692  51.209  1.00 27.92           C  
ANISOU 3867  CD2 TRP B 175     3293   3166   4149   -397    595   -130       C  
ATOM   3868  NE1 TRP B 175     -30.796  17.680  52.933  1.00 26.45           N  
ANISOU 3868  NE1 TRP B 175     3191   2921   3935   -358    678    -52       N  
ATOM   3869  CE2 TRP B 175     -30.969  17.628  51.570  1.00 27.46           C  
ANISOU 3869  CE2 TRP B 175     3275   3065   4093   -395    632   -105       C  
ATOM   3870  CE3 TRP B 175     -32.162  18.860  49.861  1.00 29.71           C  
ANISOU 3870  CE3 TRP B 175     3469   3422   4396   -427    543   -182       C  
ATOM   3871  CZ2 TRP B 175     -30.450  16.728  50.625  1.00 26.54           C  
ANISOU 3871  CZ2 TRP B 175     3151   2929   4004   -426    621   -133       C  
ATOM   3872  CZ3 TRP B 175     -31.637  17.969  48.920  1.00 27.11           C  
ANISOU 3872  CZ3 TRP B 175     3133   3079   4089   -457    529   -213       C  
ATOM   3873  CH2 TRP B 175     -30.789  16.922  49.312  1.00 30.88           C  
ANISOU 3873  CH2 TRP B 175     3653   3509   4573   -457    569   -189       C  
ATOM   3874  N   SER B 176     -30.578  21.973  54.738  1.00 25.39           N  
ANISOU 3874  N   SER B 176     3122   2908   3618   -240    584    -11       N  
ATOM   3875  CA  SER B 176     -29.471  22.882  55.043  1.00 21.48           C  
ANISOU 3875  CA  SER B 176     2672   2438   3051   -206    539     -1       C  
ATOM   3876  C   SER B 176     -29.974  24.283  55.354  1.00 26.27           C  
ANISOU 3876  C   SER B 176     3272   3074   3633   -185    520     -8       C  
ATOM   3877  O   SER B 176     -31.157  24.486  55.659  1.00 24.81           O  
ANISOU 3877  O   SER B 176     3058   2889   3478   -187    554    -10       O  
ATOM   3878  CB  SER B 176     -28.453  22.917  53.895  1.00 24.36           C  
ANISOU 3878  CB  SER B 176     3039   2813   3405   -220    478    -22       C  
ATOM   3879  OG  SER B 176     -27.273  23.625  54.274  1.00 26.64           O  
ANISOU 3879  OG  SER B 176     3372   3120   3631   -189    442    -10       O  
ATOM   3880  N   ARG B 177     -29.068  25.256  55.353  1.00 22.90           N  
ANISOU 3880  N   ARG B 177     2875   2670   3155   -163    472    -12       N  
ATOM   3881  CA  ARG B 177     -29.444  26.629  55.635  1.00 21.39           C  
ANISOU 3881  CA  ARG B 177     2681   2502   2942   -142    456    -21       C  
ATOM   3882  C   ARG B 177     -28.306  27.516  55.176  1.00 20.51           C  
ANISOU 3882  C   ARG B 177     2593   2409   2792   -131    395    -34       C  
ATOM   3883  O   ARG B 177     -27.163  27.062  55.053  1.00 22.55           O  
ANISOU 3883  O   ARG B 177     2877   2664   3026   -131    375    -29       O  
ATOM   3884  CB  ARG B 177     -29.701  26.861  57.126  1.00 21.27           C  
ANISOU 3884  CB  ARG B 177     2698   2487   2896   -109    502      1       C  
ATOM   3885  CG  ARG B 177     -28.522  26.399  57.991  1.00 27.45           C  
ANISOU 3885  CG  ARG B 177     3536   3270   3626    -85    508     26       C  
ATOM   3886  CD  ARG B 177     -28.866  26.546  59.457  1.00 25.09           C  
ANISOU 3886  CD  ARG B 177     3266   2976   3292    -51    558     48       C  
ATOM   3887  NE  ARG B 177     -27.808  26.063  60.333  1.00 25.02           N  
ANISOU 3887  NE  ARG B 177     3306   2973   3226    -22    565     74       N  
ATOM   3888  CZ  ARG B 177     -27.829  26.244  61.646  1.00 25.43           C  
ANISOU 3888  CZ  ARG B 177     3393   3040   3230     16    598     93       C  
ATOM   3889  NH1 ARG B 177     -28.874  26.794  62.246  1.00 26.03           N  
ANISOU 3889  NH1 ARG B 177     3460   3119   3310     27    634     91       N  
ATOM   3890  NH2 ARG B 177     -26.777  25.869  62.373  1.00 28.08           N  
ANISOU 3890  NH2 ARG B 177     3771   3389   3507     46    596    114       N  
ATOM   3891  N   TYR B 178     -28.611  28.797  54.982  1.00 22.51           N  
ANISOU 3891  N   TYR B 178     2835   2680   3039   -120    371    -50       N  
ATOM   3892  CA  TYR B 178     -27.554  29.773  54.726  1.00 22.48           C  
ANISOU 3892  CA  TYR B 178     2854   2688   3000   -108    322    -61       C  
ATOM   3893  C   TYR B 178     -27.079  30.322  56.061  1.00 20.18           C  
ANISOU 3893  C   TYR B 178     2605   2402   2659    -77    337    -55       C  
ATOM   3894  O   TYR B 178     -27.880  30.542  56.972  1.00 20.94           O  
ANISOU 3894  O   TYR B 178     2704   2498   2752    -61    376    -48       O  
ATOM   3895  CB  TYR B 178     -28.028  30.915  53.816  1.00 20.50           C  
ANISOU 3895  CB  TYR B 178     2572   2449   2768   -109    292    -79       C  
ATOM   3896  CG  TYR B 178     -28.254  30.431  52.392  1.00 20.89           C  
ANISOU 3896  CG  TYR B 178     2582   2504   2852   -135    265    -88       C  
ATOM   3897  CD1 TYR B 178     -27.178  30.069  51.583  1.00 20.26           C  
ANISOU 3897  CD1 TYR B 178     2512   2424   2761   -148    230    -93       C  
ATOM   3898  CD2 TYR B 178     -29.550  30.294  51.871  1.00 25.11           C  
ANISOU 3898  CD2 TYR B 178     3066   3046   3430   -148    277    -95       C  
ATOM   3899  CE1 TYR B 178     -27.374  29.611  50.266  1.00 21.43           C  
ANISOU 3899  CE1 TYR B 178     2625   2580   2936   -171    206   -105       C  
ATOM   3900  CE2 TYR B 178     -29.750  29.821  50.546  1.00 23.29           C  
ANISOU 3900  CE2 TYR B 178     2797   2827   3226   -172    250   -110       C  
ATOM   3901  CZ  TYR B 178     -28.651  29.484  49.764  1.00 22.84           C  
ANISOU 3901  CZ  TYR B 178     2756   2771   3153   -183    214   -115       C  
ATOM   3902  OH  TYR B 178     -28.828  29.004  48.474  1.00 22.59           O  
ANISOU 3902  OH  TYR B 178     2688   2753   3142   -205    188   -133       O  
ATOM   3903  N   ILE B 179     -25.770  30.538  56.172  1.00 19.95           N  
ANISOU 3903  N   ILE B 179     2609   2380   2592    -68    305    -59       N  
ATOM   3904  CA  ILE B 179     -25.167  30.890  57.459  1.00 20.39           C  
ANISOU 3904  CA  ILE B 179     2706   2447   2595    -39    314    -58       C  
ATOM   3905  C   ILE B 179     -23.967  31.800  57.188  1.00 20.14           C  
ANISOU 3905  C   ILE B 179     2690   2425   2538    -36    264    -80       C  
ATOM   3906  O   ILE B 179     -23.290  31.632  56.168  1.00 19.53           O  
ANISOU 3906  O   ILE B 179     2603   2344   2474    -53    230    -84       O  
ATOM   3907  CB  ILE B 179     -24.787  29.602  58.224  1.00 23.54           C  
ANISOU 3907  CB  ILE B 179     3130   2844   2971    -30    343    -30       C  
ATOM   3908  CG1 ILE B 179     -24.505  29.855  59.698  1.00 28.10           C  
ANISOU 3908  CG1 ILE B 179     3746   3440   3491      6    363    -24       C  
ATOM   3909  CG2 ILE B 179     -23.601  28.858  57.527  1.00 21.07           C  
ANISOU 3909  CG2 ILE B 179     2824   2527   2655    -43    310    -25       C  
ATOM   3910  CD1 ILE B 179     -24.405  28.546  60.518  1.00 26.59           C  
ANISOU 3910  CD1 ILE B 179     3578   3247   3280     22    406     14       C  
ATOM   3911  N   PRO B 180     -23.681  32.790  58.033  1.00 22.01           N  
ANISOU 3911  N   PRO B 180     2949   2674   2741    -14    261    -99       N  
ATOM   3912  CA  PRO B 180     -22.557  33.696  57.741  1.00 22.31           C  
ANISOU 3912  CA  PRO B 180     2996   2716   2764    -15    216   -125       C  
ATOM   3913  C   PRO B 180     -21.212  32.985  57.804  1.00 20.70           C  
ANISOU 3913  C   PRO B 180     2812   2524   2530    -15    191   -120       C  
ATOM   3914  O   PRO B 180     -21.025  32.011  58.538  1.00 20.90           O  
ANISOU 3914  O   PRO B 180     2855   2559   2526     -2    210    -99       O  
ATOM   3915  CB  PRO B 180     -22.659  34.767  58.832  1.00 20.07           C  
ANISOU 3915  CB  PRO B 180     2732   2443   2451      8    227   -150       C  
ATOM   3916  CG  PRO B 180     -24.143  34.758  59.249  1.00 22.99           C  
ANISOU 3916  CG  PRO B 180     3090   2807   2838     16    274   -137       C  
ATOM   3917  CD  PRO B 180     -24.537  33.262  59.129  1.00 20.35           C  
ANISOU 3917  CD  PRO B 180     2748   2470   2516      8    299   -101       C  
ATOM   3918  N   GLU B 181     -20.261  33.510  57.045  1.00 19.38           N  
ANISOU 3918  N   GLU B 181     2640   2354   2370    -27    150   -138       N  
ATOM   3919  CA  GLU B 181     -18.956  32.878  56.860  1.00 21.98           C  
ANISOU 3919  CA  GLU B 181     2980   2692   2680    -30    122   -133       C  
ATOM   3920  C   GLU B 181     -17.860  33.907  57.062  1.00 19.23           C  
ANISOU 3920  C   GLU B 181     2641   2354   2312    -27     88   -167       C  
ATOM   3921  O   GLU B 181     -18.063  35.087  56.794  1.00 20.80           O  
ANISOU 3921  O   GLU B 181     2831   2542   2530    -32     82   -191       O  
ATOM   3922  CB  GLU B 181     -18.793  32.295  55.430  1.00 18.89           C  
ANISOU 3922  CB  GLU B 181     2566   2284   2326    -55    106   -121       C  
ATOM   3923  CG  GLU B 181     -19.884  31.372  55.028  1.00 22.42           C  
ANISOU 3923  CG  GLU B 181     2997   2719   2804    -66    135    -98       C  
ATOM   3924  CD  GLU B 181     -19.426  30.451  53.922  1.00 22.21           C  
ANISOU 3924  CD  GLU B 181     2958   2683   2799    -87    120    -87       C  
ATOM   3925  OE1 GLU B 181     -18.757  29.445  54.233  1.00 22.56           O  
ANISOU 3925  OE1 GLU B 181     3017   2728   2825    -82    125    -71       O  
ATOM   3926  OE2 GLU B 181     -19.683  30.768  52.738  1.00 22.81           O  
ANISOU 3926  OE2 GLU B 181     3010   2753   2906   -104    103    -95       O  
ATOM   3927  N   GLY B 182     -16.685  33.452  57.485  1.00 19.83           N  
ANISOU 3927  N   GLY B 182     2732   2450   2354    -18     68   -168       N  
ATOM   3928  CA  GLY B 182     -15.517  34.331  57.512  1.00 19.28           C  
ANISOU 3928  CA  GLY B 182     2663   2389   2273    -20     31   -204       C  
ATOM   3929  C   GLY B 182     -15.692  35.424  58.553  1.00 19.63           C  
ANISOU 3929  C   GLY B 182     2719   2445   2293     -6     36   -240       C  
ATOM   3930  O   GLY B 182     -15.988  35.142  59.722  1.00 20.92           O  
ANISOU 3930  O   GLY B 182     2902   2634   2414     18     55   -238       O  
ATOM   3931  N   MET B 183     -15.518  36.691  58.114  1.00 20.21           N  
ANISOU 3931  N   MET B 183     2782   2502   2397    -21     23   -274       N  
ATOM   3932  CA  MET B 183     -15.754  37.873  58.944  1.00 20.20           C  
ANISOU 3932  CA  MET B 183     2788   2502   2385    -12     32   -316       C  
ATOM   3933  C   MET B 183     -17.236  38.139  59.170  1.00 25.82           C  
ANISOU 3933  C   MET B 183     3500   3200   3110     -3     72   -305       C  
ATOM   3934  O   MET B 183     -17.584  39.140  59.815  1.00 22.95           O  
ANISOU 3934  O   MET B 183     3143   2834   2743      5     85   -338       O  
ATOM   3935  CB  MET B 183     -15.086  39.116  58.314  1.00 19.88           C  
ANISOU 3935  CB  MET B 183     2733   2438   2382    -32     12   -353       C  
ATOM   3936  CG  MET B 183     -13.579  39.091  58.506  1.00 29.73           C  
ANISOU 3936  CG  MET B 183     3981   3706   3610    -37    -26   -380       C  
ATOM   3937  SD  MET B 183     -12.665  40.224  57.425  1.00 24.76           S  
ANISOU 3937  SD  MET B 183     3329   3041   3038    -66    -46   -409       S  
ATOM   3938  CE  MET B 183     -13.433  41.810  57.747  1.00 24.46           C  
ANISOU 3938  CE  MET B 183     3291   2971   3031    -67    -18   -449       C  
ATOM   3939  N   GLN B 184     -18.094  37.240  58.679  1.00 20.43           N  
ANISOU 3939  N   GLN B 184     2809   2509   2443     -5     92   -261       N  
ATOM   3940  CA  GLN B 184     -19.538  37.207  58.917  1.00 19.97           C  
ANISOU 3940  CA  GLN B 184     2747   2442   2398      4    132   -244       C  
ATOM   3941  C   GLN B 184     -20.292  38.202  58.050  1.00 19.86           C  
ANISOU 3941  C   GLN B 184     2711   2400   2436     -6    139   -249       C  
ATOM   3942  O   GLN B 184     -21.427  38.545  58.371  1.00 23.10           O  
ANISOU 3942  O   GLN B 184     3116   2803   2857      5    171   -246       O  
ATOM   3943  CB  GLN B 184     -19.873  37.423  60.398  1.00 20.42           C  
ANISOU 3943  CB  GLN B 184     2828   2522   2409     30    156   -261       C  
ATOM   3944  CG  GLN B 184     -19.062  36.465  61.304  1.00 24.84           C  
ANISOU 3944  CG  GLN B 184     3412   3118   2910     48    148   -252       C  
ATOM   3945  CD  GLN B 184     -19.487  34.991  61.170  1.00 28.22           C  
ANISOU 3945  CD  GLN B 184     3840   3547   3337     51    170   -200       C  
ATOM   3946  OE1 GLN B 184     -20.560  34.609  61.638  1.00 24.57           O  
ANISOU 3946  OE1 GLN B 184     3380   3082   2875     63    212   -178       O  
ATOM   3947  NE2 GLN B 184     -18.633  34.153  60.539  1.00 20.25           N  
ANISOU 3947  NE2 GLN B 184     2826   2537   2332     40    146   -182       N  
ATOM   3948  N   CYS B 185     -19.712  38.600  56.912  1.00 19.73           N  
ANISOU 3948  N   CYS B 185     2679   2366   2452    -24    113   -252       N  
ATOM   3949  CA  CYS B 185     -20.329  39.594  56.048  1.00 21.73           C  
ANISOU 3949  CA  CYS B 185     2912   2593   2753    -28    119   -252       C  
ATOM   3950  C   CYS B 185     -20.798  39.001  54.728  1.00 25.45           C  
ANISOU 3950  C   CYS B 185     3356   3058   3255    -39    113   -218       C  
ATOM   3951  O   CYS B 185     -21.255  39.744  53.855  1.00 23.32           O  
ANISOU 3951  O   CYS B 185     3067   2772   3021    -39    115   -212       O  
ATOM   3952  CB  CYS B 185     -19.363  40.757  55.812  1.00 26.03           C  
ANISOU 3952  CB  CYS B 185     3459   3120   3312    -34    101   -284       C  
ATOM   3953  SG  CYS B 185     -19.251  41.762  57.275  1.00 30.91           S  
ANISOU 3953  SG  CYS B 185     4099   3740   3906    -21    116   -335       S  
ATOM   3954  N   SER B 186     -20.695  37.682  54.568  1.00 19.27           N  
ANISOU 3954  N   SER B 186     2573   2290   2460    -47    107   -196       N  
ATOM   3955  CA  SER B 186     -21.313  36.967  53.461  1.00 18.88           C  
ANISOU 3955  CA  SER B 186     2498   2239   2436    -59    106   -169       C  
ATOM   3956  C   SER B 186     -21.902  35.693  54.037  1.00 20.22           C  
ANISOU 3956  C   SER B 186     2670   2421   2594    -59    128   -152       C  
ATOM   3957  O   SER B 186     -21.585  35.296  55.166  1.00 20.04           O  
ANISOU 3957  O   SER B 186     2672   2408   2536    -49    140   -154       O  
ATOM   3958  CB  SER B 186     -20.320  36.654  52.315  1.00 20.70           C  
ANISOU 3958  CB  SER B 186     2723   2468   2675    -75     73   -163       C  
ATOM   3959  OG  SER B 186     -19.366  35.652  52.671  1.00 23.67           O  
ANISOU 3959  OG  SER B 186     3116   2854   3024    -81     61   -161       O  
ATOM   3960  N   CYS B 187     -22.792  35.065  53.289  1.00 21.48           N  
ANISOU 3960  N   CYS B 187     2801   2579   2780    -70    137   -134       N  
ATOM   3961  CA  CYS B 187     -23.367  33.814  53.754  1.00 20.22           C  
ANISOU 3961  CA  CYS B 187     2640   2423   2618    -74    164   -118       C  
ATOM   3962  C   CYS B 187     -23.177  32.717  52.722  1.00 18.87           C  
ANISOU 3962  C   CYS B 187     2452   2251   2465    -96    150   -107       C  
ATOM   3963  O   CYS B 187     -23.157  32.973  51.519  1.00 20.70           O  
ANISOU 3963  O   CYS B 187     2663   2485   2718   -107    125   -111       O  
ATOM   3964  CB  CYS B 187     -24.855  33.962  54.052  1.00 21.90           C  
ANISOU 3964  CB  CYS B 187     2831   2635   2853    -68    198   -113       C  
ATOM   3965  SG  CYS B 187     -25.138  34.782  55.575  1.00 20.72           S  
ANISOU 3965  SG  CYS B 187     2708   2488   2676    -40    229   -123       S  
ATOM   3966  N   GLY B 188     -23.109  31.486  53.222  1.00 21.56           N  
ANISOU 3966  N   GLY B 188     2804   2590   2798   -100    170    -93       N  
ATOM   3967  CA  GLY B 188     -22.977  30.322  52.381  1.00 21.95           C  
ANISOU 3967  CA  GLY B 188     2840   2634   2867   -122    166    -86       C  
ATOM   3968  C   GLY B 188     -23.748  29.155  52.967  1.00 20.62           C  
ANISOU 3968  C   GLY B 188     2668   2455   2713   -127    210    -71       C  
ATOM   3969  O   GLY B 188     -24.489  29.304  53.948  1.00 20.63           O  
ANISOU 3969  O   GLY B 188     2674   2456   2710   -113    245    -63       O  
ATOM   3970  N   ILE B 189     -23.578  27.985  52.357  1.00 19.10           N  
ANISOU 3970  N   ILE B 189     2466   2252   2540   -147    213    -66       N  
ATOM   3971  CA  ILE B 189     -24.191  26.756  52.857  1.00 19.41           C  
ANISOU 3971  CA  ILE B 189     2502   2273   2599   -155    261    -50       C  
ATOM   3972  C   ILE B 189     -23.565  26.391  54.196  1.00 22.00           C  
ANISOU 3972  C   ILE B 189     2872   2598   2888   -128    287    -26       C  
ATOM   3973  O   ILE B 189     -22.386  26.690  54.460  1.00 22.43           O  
ANISOU 3973  O   ILE B 189     2955   2664   2903   -112    260    -24       O  
ATOM   3974  CB  ILE B 189     -23.970  25.658  51.794  1.00 19.34           C  
ANISOU 3974  CB  ILE B 189     2476   2251   2622   -183    254    -57       C  
ATOM   3975  CG1 ILE B 189     -24.724  26.056  50.532  1.00 25.17           C  
ANISOU 3975  CG1 ILE B 189     3170   3002   3392   -205    229    -83       C  
ATOM   3976  CG2 ILE B 189     -24.335  24.245  52.317  1.00 23.20           C  
ANISOU 3976  CG2 ILE B 189     2967   2712   3135   -192    308    -39       C  
ATOM   3977  CD1 ILE B 189     -26.199  26.194  50.787  1.00 26.89           C  
ANISOU 3977  CD1 ILE B 189     3355   3222   3642   -210    259    -87       C  
ATOM   3978  N   ASP B 190     -24.338  25.730  55.060  1.00 22.53           N  
ANISOU 3978  N   ASP B 190     2942   2653   2965   -122    340     -6       N  
ATOM   3979  CA  ASP B 190     -23.819  25.408  56.390  1.00 25.78           C  
ANISOU 3979  CA  ASP B 190     3394   3067   3332    -90    368     22       C  
ATOM   3980  C   ASP B 190     -22.899  24.183  56.287  1.00 23.18           C  
ANISOU 3980  C   ASP B 190     3083   2723   3001    -90    375     43       C  
ATOM   3981  O   ASP B 190     -23.333  23.036  56.404  1.00 26.46           O  
ANISOU 3981  O   ASP B 190     3495   3111   3448    -98    422     64       O  
ATOM   3982  CB  ASP B 190     -24.972  25.213  57.381  1.00 21.74           C  
ANISOU 3982  CB  ASP B 190     2883   2549   2830    -78    427     40       C  
ATOM   3983  CG  ASP B 190     -24.490  25.083  58.838  1.00 24.05           C  
ANISOU 3983  CG  ASP B 190     3219   2854   3064    -36    455     70       C  
ATOM   3984  OD1 ASP B 190     -23.262  25.030  59.073  1.00 22.69           O  
ANISOU 3984  OD1 ASP B 190     3076   2696   2848    -17    427     76       O  
ATOM   3985  OD2 ASP B 190     -25.343  25.037  59.738  1.00 26.69           O  
ANISOU 3985  OD2 ASP B 190     3559   3187   3396    -20    504     86       O  
ATOM   3986  N   TYR B 191     -21.585  24.449  56.114  1.00 22.71           N  
ANISOU 3986  N   TYR B 191     3043   2678   2906    -79    330     39       N  
ATOM   3987  CA  TYR B 191     -20.509  23.453  56.243  1.00 27.78           C  
ANISOU 3987  CA  TYR B 191     3708   3313   3533    -68    334     62       C  
ATOM   3988  C   TYR B 191     -20.089  23.219  57.683  1.00 26.68           C  
ANISOU 3988  C   TYR B 191     3607   3190   3341    -24    359     95       C  
ATOM   3989  O   TYR B 191     -19.268  22.321  57.935  1.00 24.99           O  
ANISOU 3989  O   TYR B 191     3413   2971   3112     -7    369    122       O  
ATOM   3990  CB  TYR B 191     -19.245  23.888  55.466  1.00 20.51           C  
ANISOU 3990  CB  TYR B 191     2790   2407   2596    -72    274     43       C  
ATOM   3991  CG  TYR B 191     -19.597  24.627  54.198  1.00 24.64           C  
ANISOU 3991  CG  TYR B 191     3281   2930   3152   -104    239      9       C  
ATOM   3992  CD1 TYR B 191     -20.276  23.986  53.166  1.00 20.73           C  
ANISOU 3992  CD1 TYR B 191     2757   2413   2708   -136    250     -1       C  
ATOM   3993  CD2 TYR B 191     -19.264  25.964  54.035  1.00 21.60           C  
ANISOU 3993  CD2 TYR B 191     2894   2566   2746   -100    198    -15       C  
ATOM   3994  CE1 TYR B 191     -20.631  24.651  52.012  1.00 22.77           C  
ANISOU 3994  CE1 TYR B 191     2985   2678   2988   -159    217    -30       C  
ATOM   3995  CE2 TYR B 191     -19.602  26.644  52.849  1.00 20.24           C  
ANISOU 3995  CE2 TYR B 191     2694   2395   2602   -123    169    -39       C  
ATOM   3996  CZ  TYR B 191     -20.293  25.976  51.855  1.00 23.31           C  
ANISOU 3996  CZ  TYR B 191     3055   2769   3034   -150    178    -45       C  
ATOM   3997  OH  TYR B 191     -20.679  26.650  50.716  1.00 25.20           O  
ANISOU 3997  OH  TYR B 191     3265   3015   3294   -167    150    -67       O  
ATOM   3998  N   TYR B 192     -20.616  24.007  58.619  1.00 20.49           N  
ANISOU 3998  N   TYR B 192     2833   2427   2527     -3    370     93       N  
ATOM   3999  CA  TYR B 192     -19.976  24.248  59.903  1.00 27.11           C  
ANISOU 3999  CA  TYR B 192     3706   3298   3296     41    371    108       C  
ATOM   4000  C   TYR B 192     -20.543  23.408  61.009  1.00 30.64           C  
ANISOU 4000  C   TYR B 192     4174   3739   3729     70    436    152       C  
ATOM   4001  O   TYR B 192     -19.807  23.045  61.928  1.00 25.70           O  
ANISOU 4001  O   TYR B 192     3580   3136   3049    111    444    180       O  
ATOM   4002  CB  TYR B 192     -20.120  25.721  60.305  1.00 24.14           C  
ANISOU 4002  CB  TYR B 192     3332   2952   2889     50    342     74       C  
ATOM   4003  CG  TYR B 192     -19.444  26.620  59.296  1.00 22.27           C  
ANISOU 4003  CG  TYR B 192     3078   2721   2664     26    280     34       C  
ATOM   4004  CD1 TYR B 192     -18.112  26.964  59.444  1.00 20.27           C  
ANISOU 4004  CD1 TYR B 192     2838   2492   2370     40    236     22       C  
ATOM   4005  CD2 TYR B 192     -20.145  27.090  58.185  1.00 19.94           C  
ANISOU 4005  CD2 TYR B 192     2750   2406   2421     -9    269     12       C  
ATOM   4006  CE1 TYR B 192     -17.474  27.788  58.480  1.00 20.53           C  
ANISOU 4006  CE1 TYR B 192     2855   2526   2420     17    186    -12       C  
ATOM   4007  CE2 TYR B 192     -19.546  27.903  57.248  1.00 20.21           C  
ANISOU 4007  CE2 TYR B 192     2770   2443   2465    -27    219    -18       C  
ATOM   4008  CZ  TYR B 192     -18.208  28.244  57.395  1.00 21.38           C  
ANISOU 4008  CZ  TYR B 192     2934   2611   2578    -15    180    -29       C  
ATOM   4009  OH  TYR B 192     -17.613  29.036  56.438  1.00 21.04           O  
ANISOU 4009  OH  TYR B 192     2877   2567   2551    -34    137    -56       O  
ATOM   4010  N   THR B 193     -21.841  23.129  60.959  1.00 28.55           N  
ANISOU 4010  N   THR B 193     3892   3447   3511     53    485    159       N  
ATOM   4011  CA  THR B 193     -22.513  22.492  62.073  1.00 31.21           C  
ANISOU 4011  CA  THR B 193     4248   3777   3836     81    555    200       C  
ATOM   4012  C   THR B 193     -23.315  21.299  61.571  1.00 30.70           C  
ANISOU 4012  C   THR B 193     4161   3660   3844     53    611    222       C  
ATOM   4013  O   THR B 193     -23.699  21.242  60.401  1.00 32.36           O  
ANISOU 4013  O   THR B 193     4335   3847   4115      8    594    193       O  
ATOM   4014  CB  THR B 193     -23.436  23.472  62.819  1.00 30.00           C  
ANISOU 4014  CB  THR B 193     4094   3643   3663     94    570    187       C  
ATOM   4015  OG1 THR B 193     -24.645  23.694  62.080  1.00 30.57           O  
ANISOU 4015  OG1 THR B 193     4126   3688   3801     54    585    165       O  
ATOM   4016  CG2 THR B 193     -22.740  24.842  63.056  1.00 29.58           C  
ANISOU 4016  CG2 THR B 193     4053   3634   3554    109    509    148       C  
ATOM   4017  N   PRO B 194     -23.551  20.313  62.434  1.00 34.18           N  
ANISOU 4017  N   PRO B 194     4622   4083   4281     79    679    271       N  
ATOM   4018  CA  PRO B 194     -24.400  19.191  62.011  1.00 43.88           C  
ANISOU 4018  CA  PRO B 194     5828   5257   5589     49    741    288       C  
ATOM   4019  C   PRO B 194     -25.846  19.601  61.803  1.00 40.40           C  
ANISOU 4019  C   PRO B 194     5350   4802   5199     17    767    264       C  
ATOM   4020  O   PRO B 194     -26.494  19.120  60.864  1.00 54.24           O  
ANISOU 4020  O   PRO B 194     7063   6520   7027    -29    778    244       O  
ATOM   4021  CB  PRO B 194     -24.251  18.185  63.163  1.00 46.62           C  
ANISOU 4021  CB  PRO B 194     6212   5591   5910     94    812    353       C  
ATOM   4022  CG  PRO B 194     -23.039  18.648  63.946  1.00 47.94           C  
ANISOU 4022  CG  PRO B 194     6420   5812   5982    147    771    367       C  
ATOM   4023  CD  PRO B 194     -22.988  20.123  63.781  1.00 42.17           C  
ANISOU 4023  CD  PRO B 194     5680   5124   5218    139    703    315       C  
ATOM   4024  N   HIS B 195     -26.376  20.426  62.704  1.00 30.06           N  
ANISOU 4024  N   HIS B 195     4051   3520   3851     44    779    266       N  
ATOM   4025  CA  HIS B 195     -27.751  20.924  62.720  1.00 35.07           C  
ANISOU 4025  CA  HIS B 195     4652   4148   4525     24    807    249       C  
ATOM   4026  C   HIS B 195     -28.748  19.923  62.144  1.00 40.78           C  
ANISOU 4026  C   HIS B 195     5336   4820   5340    -18    862    252       C  
ATOM   4027  O   HIS B 195     -29.215  20.099  61.013  1.00 34.94           O  
ANISOU 4027  O   HIS B 195     4550   4071   4656    -63    831    210       O  
ATOM   4028  CB  HIS B 195     -27.906  22.278  62.047  1.00 33.29           C  
ANISOU 4028  CB  HIS B 195     4402   3950   4296      6    740    196       C  
ATOM   4029  CG  HIS B 195     -29.080  23.031  62.586  1.00 33.84           C  
ANISOU 4029  CG  HIS B 195     4457   4030   4373     12    770    188       C  
ATOM   4030  ND1 HIS B 195     -30.192  23.336  61.831  1.00 36.95           N  
ANISOU 4030  ND1 HIS B 195     4799   4411   4830    -24    771    160       N  
ATOM   4031  CD2 HIS B 195     -29.343  23.472  63.840  1.00 31.44           C  
ANISOU 4031  CD2 HIS B 195     4182   3746   4018     53    804    208       C  
ATOM   4032  CE1 HIS B 195     -31.075  23.966  62.591  1.00 38.04           C  
ANISOU 4032  CE1 HIS B 195     4935   4560   4961     -6    804    162       C  
ATOM   4033  NE2 HIS B 195     -30.582  24.062  63.813  1.00 37.19           N  
ANISOU 4033  NE2 HIS B 195     4877   4471   4783     40    826    190       N  
ATOM   4034  N   GLU B 196     -28.995  18.822  62.859  1.00 40.06           N  
ANISOU 4034  N   GLU B 196     5260   4695   5265     -2    941    300       N  
ATOM   4035  CA  GLU B 196     -29.794  17.740  62.289  1.00 39.51           C  
ANISOU 4035  CA  GLU B 196     5153   4570   5290    -46    996    300       C  
ATOM   4036  C   GLU B 196     -31.209  18.172  61.922  1.00 33.18           C  
ANISOU 4036  C   GLU B 196     4296   3762   4550    -82   1012    266       C  
ATOM   4037  O   GLU B 196     -31.828  17.531  61.067  1.00 35.13           O  
ANISOU 4037  O   GLU B 196     4496   3974   4878   -131   1028    242       O  
ATOM   4038  CB  GLU B 196     -29.856  16.555  63.253  1.00 40.37           C  
ANISOU 4038  CB  GLU B 196     5291   4641   5407    -18   1090    364       C  
ATOM   4039  CG  GLU B 196     -28.554  15.759  63.312  1.00 56.25           C  
ANISOU 4039  CG  GLU B 196     7343   6644   7387      8   1084    398       C  
ATOM   4040  CD  GLU B 196     -27.508  16.422  64.191  1.00 67.91           C  
ANISOU 4040  CD  GLU B 196     8872   8177   8755     69   1045    421       C  
ATOM   4041  OE1 GLU B 196     -27.809  17.492  64.785  1.00 61.00           O  
ANISOU 4041  OE1 GLU B 196     8004   7345   7829     90   1025    410       O  
ATOM   4042  OE2 GLU B 196     -26.389  15.866  64.296  1.00 66.24           O  
ANISOU 4042  OE2 GLU B 196     8691   7967   8509     96   1034    450       O  
ATOM   4043  N   GLU B 197     -31.735  19.231  62.542  1.00 30.11           N  
ANISOU 4043  N   GLU B 197     3909   3407   4123    -59   1007    262       N  
ATOM   4044  CA  GLU B 197     -33.084  19.671  62.192  1.00 33.31           C  
ANISOU 4044  CA  GLU B 197     4260   3810   4588    -90   1020    231       C  
ATOM   4045  C   GLU B 197     -33.198  20.031  60.707  1.00 40.95           C  
ANISOU 4045  C   GLU B 197     5176   4784   5598   -138    950    173       C  
ATOM   4046  O   GLU B 197     -34.273  19.900  60.114  1.00 35.13           O  
ANISOU 4046  O   GLU B 197     4382   4034   4933   -176    966    146       O  
ATOM   4047  CB  GLU B 197     -33.485  20.862  63.047  1.00 38.24           C  
ANISOU 4047  CB  GLU B 197     4899   4472   5160    -54   1019    233       C  
ATOM   4048  CG  GLU B 197     -34.950  21.239  62.914  1.00 65.62           C  
ANISOU 4048  CG  GLU B 197     8312   7934   8688    -77   1049    212       C  
ATOM   4049  CD  GLU B 197     -35.317  22.423  63.785  1.00 72.32           C  
ANISOU 4049  CD  GLU B 197     9177   8817   9483    -39   1051    214       C  
ATOM   4050  OE1 GLU B 197     -34.393  23.155  64.200  1.00 67.14           O  
ANISOU 4050  OE1 GLU B 197     8568   8196   8748     -4   1007    214       O  
ATOM   4051  OE2 GLU B 197     -36.521  22.618  64.061  1.00 79.40           O  
ANISOU 4051  OE2 GLU B 197    10041   9708  10421    -44   1098    213       O  
ATOM   4052  N   THR B 198     -32.113  20.484  60.089  1.00 31.91           N  
ANISOU 4052  N   THR B 198     4049   3664   4411   -135    874    154       N  
ATOM   4053  CA  THR B 198     -32.121  20.801  58.659  1.00 28.01           C  
ANISOU 4053  CA  THR B 198     3512   3181   3950   -175    808    104       C  
ATOM   4054  C   THR B 198     -31.331  19.790  57.838  1.00 25.85           C  
ANISOU 4054  C   THR B 198     3240   2882   3699   -200    794     97       C  
ATOM   4055  O   THR B 198     -31.038  20.046  56.661  1.00 28.36           O  
ANISOU 4055  O   THR B 198     3534   3215   4028   -226    732     59       O  
ATOM   4056  CB  THR B 198     -31.578  22.209  58.427  1.00 30.18           C  
ANISOU 4056  CB  THR B 198     3800   3501   4167   -155    733     82       C  
ATOM   4057  OG1 THR B 198     -30.348  22.358  59.144  1.00 28.98           O  
ANISOU 4057  OG1 THR B 198     3708   3363   3942   -117    718    108       O  
ATOM   4058  CG2 THR B 198     -32.574  23.264  58.879  1.00 29.75           C  
ANISOU 4058  CG2 THR B 198     3727   3468   4109   -141    743     74       C  
ATOM   4059  N   ASN B 199     -30.957  18.653  58.433  1.00 25.96           N  
ANISOU 4059  N   ASN B 199     3283   2860   3720   -190    851    136       N  
ATOM   4060  CA  ASN B 199     -30.318  17.561  57.693  1.00 28.46           C  
ANISOU 4060  CA  ASN B 199     3599   3144   4070   -216    850    131       C  
ATOM   4061  C   ASN B 199     -29.122  18.062  56.893  1.00 29.08           C  
ANISOU 4061  C   ASN B 199     3693   3252   4104   -213    767    109       C  
ATOM   4062  O   ASN B 199     -28.953  17.767  55.705  1.00 27.99           O  
ANISOU 4062  O   ASN B 199     3527   3108   3999   -249    732     72       O  
ATOM   4063  CB  ASN B 199     -31.335  16.859  56.796  1.00 27.66           C  
ANISOU 4063  CB  ASN B 199     3435   3011   4062   -272    875     93       C  
ATOM   4064  CG  ASN B 199     -32.326  16.054  57.605  1.00 45.53           C  
ANISOU 4064  CG  ASN B 199     5687   5231   6380   -277    971    120       C  
ATOM   4065  OD1 ASN B 199     -33.524  16.334  57.606  1.00 49.43           O  
ANISOU 4065  OD1 ASN B 199     6135   5727   6917   -297    993    101       O  
ATOM   4066  ND2 ASN B 199     -31.820  15.081  58.342  1.00 35.04           N  
ANISOU 4066  ND2 ASN B 199     4400   3864   5051   -256   1033    170       N  
ATOM   4067  N   ASN B 200     -28.258  18.808  57.585  1.00 27.41           N  
ANISOU 4067  N   ASN B 200     3527   3073   3814   -169    737    131       N  
ATOM   4068  CA  ASN B 200     -27.178  19.528  56.915  1.00 24.58           C  
ANISOU 4068  CA  ASN B 200     3182   2748   3412   -164    657    108       C  
ATOM   4069  C   ASN B 200     -26.258  18.594  56.153  1.00 27.45           C  
ANISOU 4069  C   ASN B 200     3551   3088   3791   -180    644    106       C  
ATOM   4070  O   ASN B 200     -25.789  18.933  55.053  1.00 25.28           O  
ANISOU 4070  O   ASN B 200     3260   2828   3517   -201    585     71       O  
ATOM   4071  CB  ASN B 200     -26.348  20.296  57.947  1.00 28.74           C  
ANISOU 4071  CB  ASN B 200     3756   3308   3855   -114    638    133       C  
ATOM   4072  CG  ASN B 200     -26.970  21.589  58.356  1.00 31.07           C  
ANISOU 4072  CG  ASN B 200     4044   3635   4125   -101    621    118       C  
ATOM   4073  OD1 ASN B 200     -28.102  21.913  57.965  1.00 30.50           O  
ANISOU 4073  OD1 ASN B 200     3932   3560   4098   -125    630     96       O  
ATOM   4074  ND2 ASN B 200     -26.231  22.369  59.161  1.00 27.20           N  
ANISOU 4074  ND2 ASN B 200     3593   3178   3565    -62    597    128       N  
ATOM   4075  N   GLU B 201     -25.900  17.458  56.759  1.00 23.82           N  
ANISOU 4075  N   GLU B 201     3118   2594   3338   -166    699    146       N  
ATOM   4076  CA  GLU B 201     -24.853  16.638  56.168  1.00 28.74           C  
ANISOU 4076  CA  GLU B 201     3755   3198   3968   -171    687    149       C  
ATOM   4077  C   GLU B 201     -25.276  16.116  54.807  1.00 24.36           C  
ANISOU 4077  C   GLU B 201     3155   2619   3482   -226    677    102       C  
ATOM   4078  O   GLU B 201     -24.485  16.125  53.850  1.00 28.95           O  
ANISOU 4078  O   GLU B 201     3734   3208   4058   -239    628     78       O  
ATOM   4079  CB  GLU B 201     -24.492  15.472  57.099  1.00 30.48           C  
ANISOU 4079  CB  GLU B 201     4011   3382   4189   -142    757    206       C  
ATOM   4080  CG  GLU B 201     -23.531  14.471  56.452  1.00 34.15           C  
ANISOU 4080  CG  GLU B 201     4485   3816   4673   -150    757    210       C  
ATOM   4081  CD  GLU B 201     -23.629  13.084  57.067  1.00 59.92           C  
ANISOU 4081  CD  GLU B 201     7767   7024   7977   -138    846    258       C  
ATOM   4082  OE1 GLU B 201     -23.118  12.902  58.195  1.00 53.77           O  
ANISOU 4082  OE1 GLU B 201     7030   6252   7148    -84    875    315       O  
ATOM   4083  OE2 GLU B 201     -24.238  12.189  56.425  1.00 61.57           O  
ANISOU 4083  OE2 GLU B 201     7946   7182   8266   -181    887    237       O  
ATOM   4084  N   SER B 202     -26.529  15.670  54.683  1.00 24.08           N  
ANISOU 4084  N   SER B 202     3081   2556   3513   -259    724     87       N  
ATOM   4085  CA  SER B 202     -26.941  15.105  53.400  1.00 29.52           C  
ANISOU 4085  CA  SER B 202     3724   3225   4267   -312    715     36       C  
ATOM   4086  C   SER B 202     -26.967  16.174  52.321  1.00 24.29           C  
ANISOU 4086  C   SER B 202     3032   2611   3586   -328    633    -13       C  
ATOM   4087  O   SER B 202     -26.678  15.894  51.151  1.00 28.26           O  
ANISOU 4087  O   SER B 202     3515   3114   4108   -358    598    -52       O  
ATOM   4088  CB  SER B 202     -28.315  14.437  53.520  1.00 28.52           C  
ANISOU 4088  CB  SER B 202     3555   3062   4218   -346    782     24       C  
ATOM   4089  OG  SER B 202     -29.279  15.373  53.939  1.00 27.62           O  
ANISOU 4089  OG  SER B 202     3420   2978   4096   -340    778     20       O  
ATOM   4090  N   PHE B 203     -27.318  17.407  52.687  1.00 23.36           N  
ANISOU 4090  N   PHE B 203     2913   2534   3429   -308    603    -11       N  
ATOM   4091  CA  PHE B 203     -27.358  18.434  51.660  1.00 23.62           C  
ANISOU 4091  CA  PHE B 203     2919   2610   3446   -320    530    -52       C  
ATOM   4092  C   PHE B 203     -25.963  18.701  51.102  1.00 24.19           C  
ANISOU 4092  C   PHE B 203     3021   2699   3472   -307    475    -53       C  
ATOM   4093  O   PHE B 203     -25.797  18.866  49.891  1.00 25.60           O  
ANISOU 4093  O   PHE B 203     3175   2894   3656   -328    428    -89       O  
ATOM   4094  CB  PHE B 203     -27.983  19.735  52.181  1.00 28.06           C  
ANISOU 4094  CB  PHE B 203     3475   3208   3979   -298    514    -48       C  
ATOM   4095  CG  PHE B 203     -27.998  20.805  51.130  1.00 22.51           C  
ANISOU 4095  CG  PHE B 203     2747   2546   3260   -304    445    -82       C  
ATOM   4096  CD1 PHE B 203     -26.905  21.630  50.957  1.00 23.48           C  
ANISOU 4096  CD1 PHE B 203     2901   2694   3328   -281    393    -77       C  
ATOM   4097  CD2 PHE B 203     -29.062  20.902  50.234  1.00 26.35           C  
ANISOU 4097  CD2 PHE B 203     3175   3046   3789   -334    432   -121       C  
ATOM   4098  CE1 PHE B 203     -26.865  22.574  49.916  1.00 23.22           C  
ANISOU 4098  CE1 PHE B 203     2845   2694   3282   -285    333   -104       C  
ATOM   4099  CE2 PHE B 203     -29.046  21.842  49.208  1.00 23.08           C  
ANISOU 4099  CE2 PHE B 203     2738   2672   3357   -335    369   -148       C  
ATOM   4100  CZ  PHE B 203     -27.953  22.682  49.048  1.00 26.01           C  
ANISOU 4100  CZ  PHE B 203     3145   3064   3674   -310    322   -137       C  
ATOM   4101  N   VAL B 204     -24.948  18.774  51.968  1.00 26.08           N  
ANISOU 4101  N   VAL B 204     3310   2939   3662   -269    478    -14       N  
ATOM   4102  CA  VAL B 204     -23.602  19.088  51.480  1.00 21.58           C  
ANISOU 4102  CA  VAL B 204     2765   2386   3050   -256    425    -15       C  
ATOM   4103  C   VAL B 204     -23.123  18.012  50.514  1.00 25.22           C  
ANISOU 4103  C   VAL B 204     3217   2820   3544   -283    427    -33       C  
ATOM   4104  O   VAL B 204     -22.538  18.317  49.474  1.00 21.74           O  
ANISOU 4104  O   VAL B 204     2768   2397   3093   -294    377    -59       O  
ATOM   4105  CB  VAL B 204     -22.635  19.264  52.671  1.00 24.28           C  
ANISOU 4105  CB  VAL B 204     3157   2735   3335   -211    431     28       C  
ATOM   4106  CG1 VAL B 204     -21.239  19.591  52.182  1.00 28.54           C  
ANISOU 4106  CG1 VAL B 204     3715   3292   3835   -199    378     24       C  
ATOM   4107  CG2 VAL B 204     -23.122  20.401  53.581  1.00 22.66           C  
ANISOU 4107  CG2 VAL B 204     2958   2558   3093   -186    427     36       C  
ATOM   4108  N  AILE B 205     -23.365  16.740  50.842  0.33 25.31           N  
ANISOU 4108  N  AILE B 205     3232   2787   3599   -294    488    -18       N  
ATOM   4109  N  BILE B 205     -23.366  16.738  50.840  0.67 25.30           N  
ANISOU 4109  N  BILE B 205     3230   2786   3598   -294    488    -18       N  
ATOM   4110  CA AILE B 205     -22.985  15.652  49.938  0.33 23.72           C  
ANISOU 4110  CA AILE B 205     3021   2554   3438   -322    498    -39       C  
ATOM   4111  CA BILE B 205     -22.979  15.649  49.934  0.67 23.64           C  
ANISOU 4111  CA BILE B 205     3010   2543   3427   -322    497    -39       C  
ATOM   4112  C  AILE B 205     -23.718  15.796  48.611  0.33 25.15           C  
ANISOU 4112  C  AILE B 205     3152   2749   3655   -365    466    -99       C  
ATOM   4113  C  BILE B 205     -23.723  15.780  48.610  0.67 25.09           C  
ANISOU 4113  C  BILE B 205     3143   2741   3647   -366    466    -99       C  
ATOM   4114  O  AILE B 205     -23.128  15.660  47.532  0.33 28.71           O  
ANISOU 4114  O  AILE B 205     3596   3208   4104   -380    429   -128       O  
ATOM   4115  O  BILE B 205     -23.142  15.623  47.529  0.67 28.89           O  
ANISOU 4115  O  BILE B 205     3619   3230   4129   -381    431   -128       O  
ATOM   4116  CB AILE B 205     -23.272  14.287  50.590  0.33 24.36           C  
ANISOU 4116  CB AILE B 205     3111   2577   3568   -326    580    -12       C  
ATOM   4117  CB BILE B 205     -23.235  14.280  50.601  0.67 24.31           C  
ANISOU 4117  CB BILE B 205     3106   2571   3561   -325    579    -12       C  
ATOM   4118  CG1AILE B 205     -22.543  14.165  51.932  0.33 27.60           C  
ANISOU 4118  CG1AILE B 205     3572   2981   3934   -274    610     52       C  
ATOM   4119  CG1BILE B 205     -22.313  14.092  51.817  0.67 27.61           C  
ANISOU 4119  CG1BILE B 205     3577   2982   3933   -273    605     52       C  
ATOM   4120  CG2AILE B 205     -22.880  13.163  49.640  0.33 25.38           C  
ANISOU 4120  CG2AILE B 205     3231   2670   3744   -356    592    -39       C  
ATOM   4121  CG2BILE B 205     -23.007  13.171  49.583  0.67 25.36           C  
ANISOU 4121  CG2BILE B 205     3224   2667   3746   -360    592    -44       C  
ATOM   4122  CD1AILE B 205     -21.035  14.251  51.841  0.33 24.38           C  
ANISOU 4122  CD1AILE B 205     3198   2588   3475   -245    571     70       C  
ATOM   4123  CD1BILE B 205     -22.719  12.943  52.792  0.67 27.05           C  
ANISOU 4123  CD1BILE B 205     3521   2858   3900   -263    696     95       C  
ATOM   4124  N   TYR B 206     -25.020  16.083  48.677  1.00 26.36           N  
ANISOU 4124  N   TYR B 206     3268   2911   3838   -384    479   -118       N  
ATOM   4125  CA  TYR B 206     -25.806  16.299  47.468  1.00 29.58           C  
ANISOU 4125  CA  TYR B 206     3622   3343   4275   -420    445   -174       C  
ATOM   4126  C   TYR B 206     -25.257  17.457  46.645  1.00 27.99           C  
ANISOU 4126  C   TYR B 206     3420   3193   4020   -407    368   -189       C  
ATOM   4127  O   TYR B 206     -25.090  17.344  45.426  1.00 26.67           O  
ANISOU 4127  O   TYR B 206     3233   3043   3859   -428    332   -228       O  
ATOM   4128  CB  TYR B 206     -27.255  16.568  47.873  1.00 26.65           C  
ANISOU 4128  CB  TYR B 206     3211   2977   3937   -433    471   -184       C  
ATOM   4129  CG  TYR B 206     -28.067  17.353  46.864  1.00 30.35           C  
ANISOU 4129  CG  TYR B 206     3628   3493   4410   -451    420   -230       C  
ATOM   4130  CD1 TYR B 206     -28.507  16.760  45.694  1.00 26.52           C  
ANISOU 4130  CD1 TYR B 206     3097   3014   3966   -492    406   -286       C  
ATOM   4131  CD2 TYR B 206     -28.427  18.681  47.110  1.00 29.22           C  
ANISOU 4131  CD2 TYR B 206     3481   3392   4231   -425    387   -218       C  
ATOM   4132  CE1 TYR B 206     -29.288  17.438  44.795  1.00 28.15           C  
ANISOU 4132  CE1 TYR B 206     3253   3270   4173   -504    359   -326       C  
ATOM   4133  CE2 TYR B 206     -29.193  19.388  46.195  1.00 28.59           C  
ANISOU 4133  CE2 TYR B 206     3352   3357   4155   -436    343   -255       C  
ATOM   4134  CZ  TYR B 206     -29.628  18.746  45.047  1.00 31.93           C  
ANISOU 4134  CZ  TYR B 206     3728   3788   4614   -474    329   -308       C  
ATOM   4135  OH  TYR B 206     -30.389  19.426  44.141  1.00 29.05           O  
ANISOU 4135  OH  TYR B 206     3314   3476   4249   -480    283   -342       O  
ATOM   4136  N   MET B 207     -24.929  18.565  47.301  1.00 25.09           N  
ANISOU 4136  N   MET B 207     3079   2851   3603   -371    346   -159       N  
ATOM   4137  CA  MET B 207     -24.405  19.707  46.565  1.00 19.98           C  
ANISOU 4137  CA  MET B 207     2433   2248   2912   -358    280   -169       C  
ATOM   4138  C   MET B 207     -23.068  19.380  45.899  1.00 25.61           C  
ANISOU 4138  C   MET B 207     3171   2956   3602   -356    254   -171       C  
ATOM   4139  O   MET B 207     -22.874  19.651  44.713  1.00 24.46           O  
ANISOU 4139  O   MET B 207     3008   2836   3451   -367    212   -200       O  
ATOM   4140  CB  MET B 207     -24.262  20.925  47.505  1.00 19.75           C  
ANISOU 4140  CB  MET B 207     2428   2237   2837   -321    269   -138       C  
ATOM   4141  CG  MET B 207     -23.691  22.136  46.798  1.00 23.45           C  
ANISOU 4141  CG  MET B 207     2900   2744   3267   -307    209   -146       C  
ATOM   4142  SD  MET B 207     -23.514  23.560  47.903  1.00 29.76           S  
ANISOU 4142  SD  MET B 207     3726   3559   4021   -268    199   -118       S  
ATOM   4143  CE  MET B 207     -22.031  23.063  48.744  1.00 25.25           C  
ANISOU 4143  CE  MET B 207     3209   2970   3417   -246    209    -87       C  
ATOM   4144  N   PHE B 208     -22.140  18.756  46.629  1.00 22.28           N  
ANISOU 4144  N   PHE B 208     2789   2505   3170   -339    280   -138       N  
ATOM   4145  CA  PHE B 208     -20.831  18.499  46.016  1.00 23.10           C  
ANISOU 4145  CA  PHE B 208     2916   2608   3254   -334    255   -138       C  
ATOM   4146  C   PHE B 208     -20.895  17.414  44.932  1.00 29.32           C  
ANISOU 4146  C   PHE B 208     3682   3376   4082   -368    264   -175       C  
ATOM   4147  O   PHE B 208     -20.099  17.452  43.989  1.00 26.73           O  
ANISOU 4147  O   PHE B 208     3357   3060   3738   -371    230   -191       O  
ATOM   4148  CB  PHE B 208     -19.798  18.116  47.080  1.00 25.21           C  
ANISOU 4148  CB  PHE B 208     3228   2854   3497   -303    279    -94       C  
ATOM   4149  CG  PHE B 208     -19.084  19.309  47.688  1.00 19.09           C  
ANISOU 4149  CG  PHE B 208     2477   2109   2666   -268    244    -71       C  
ATOM   4150  CD1 PHE B 208     -18.060  19.928  47.019  1.00 26.83           C  
ANISOU 4150  CD1 PHE B 208     3465   3111   3616   -261    196    -78       C  
ATOM   4151  CD2 PHE B 208     -19.461  19.791  48.912  1.00 29.01           C  
ANISOU 4151  CD2 PHE B 208     3748   3372   3903   -245    262    -46       C  
ATOM   4152  CE1 PHE B 208     -17.420  21.022  47.573  1.00 31.97           C  
ANISOU 4152  CE1 PHE B 208     4135   3787   4224   -234    167    -63       C  
ATOM   4153  CE2 PHE B 208     -18.840  20.881  49.464  1.00 31.57           C  
ANISOU 4153  CE2 PHE B 208     4091   3724   4178   -217    231    -34       C  
ATOM   4154  CZ  PHE B 208     -17.824  21.487  48.800  1.00 29.88           C  
ANISOU 4154  CZ  PHE B 208     3883   3529   3941   -213    184    -44       C  
ATOM   4155  N   VAL B 209     -21.817  16.456  45.038  1.00 25.08           N  
ANISOU 4155  N   VAL B 209     3122   2808   3599   -396    311   -191       N  
ATOM   4156  CA  VAL B 209     -21.905  15.388  44.043  1.00 27.73           C  
ANISOU 4156  CA  VAL B 209     3436   3122   3978   -432    322   -233       C  
ATOM   4157  C   VAL B 209     -22.658  15.861  42.804  1.00 25.30           C  
ANISOU 4157  C   VAL B 209     3081   2856   3675   -458    278   -288       C  
ATOM   4158  O   VAL B 209     -22.149  15.808  41.676  1.00 27.37           O  
ANISOU 4158  O   VAL B 209     3337   3137   3924   -467    244   -318       O  
ATOM   4159  CB  VAL B 209     -22.583  14.141  44.652  1.00 32.95           C  
ANISOU 4159  CB  VAL B 209     4089   3728   4702   -453    396   -232       C  
ATOM   4160  CG1 VAL B 209     -22.948  13.148  43.559  1.00 32.24           C  
ANISOU 4160  CG1 VAL B 209     3966   3619   4666   -499    407   -290       C  
ATOM   4161  CG2 VAL B 209     -21.700  13.514  45.715  1.00 28.94           C  
ANISOU 4161  CG2 VAL B 209     3630   3179   4187   -423    441   -175       C  
ATOM   4162  N   VAL B 210     -23.893  16.320  43.000  1.00 20.62           N  
ANISOU 4162  N   VAL B 210     2453   2282   3098   -467    280   -300       N  
ATOM   4163  CA  VAL B 210     -24.755  16.669  41.870  1.00 22.90           C  
ANISOU 4163  CA  VAL B 210     2690   2615   3396   -490    242   -352       C  
ATOM   4164  C   VAL B 210     -24.345  18.005  41.274  1.00 24.83           C  
ANISOU 4164  C   VAL B 210     2939   2914   3580   -463    178   -345       C  
ATOM   4165  O   VAL B 210     -24.400  18.196  40.056  1.00 26.88           O  
ANISOU 4165  O   VAL B 210     3174   3212   3828   -472    137   -382       O  
ATOM   4166  CB  VAL B 210     -26.241  16.679  42.289  1.00 23.02           C  
ANISOU 4166  CB  VAL B 210     2661   2632   3454   -509    267   -367       C  
ATOM   4167  CG1 VAL B 210     -27.116  17.107  41.139  1.00 28.32           C  
ANISOU 4167  CG1 VAL B 210     3276   3358   4128   -527    222   -420       C  
ATOM   4168  CG2 VAL B 210     -26.668  15.283  42.755  1.00 29.23           C  
ANISOU 4168  CG2 VAL B 210     3438   3359   4308   -541    336   -378       C  
ATOM   4169  N   HIS B 211     -23.952  18.963  42.114  1.00 20.18           N  
ANISOU 4169  N   HIS B 211     2382   2331   2956   -428    171   -299       N  
ATOM   4170  CA  HIS B 211     -23.775  20.327  41.630  1.00 25.60           C  
ANISOU 4170  CA  HIS B 211     3067   3064   3595   -403    119   -292       C  
ATOM   4171  C   HIS B 211     -22.323  20.754  41.599  1.00 28.64           C  
ANISOU 4171  C   HIS B 211     3497   3448   3938   -378     97   -264       C  
ATOM   4172  O   HIS B 211     -22.041  21.955  41.644  1.00 22.71           O  
ANISOU 4172  O   HIS B 211     2756   2721   3150   -352     68   -244       O  
ATOM   4173  CB  HIS B 211     -24.608  21.284  42.468  1.00 25.58           C  
ANISOU 4173  CB  HIS B 211     3056   3074   3589   -385    124   -270       C  
ATOM   4174  CG  HIS B 211     -26.070  21.007  42.359  1.00 28.07           C  
ANISOU 4174  CG  HIS B 211     3320   3400   3947   -408    140   -299       C  
ATOM   4175  ND1 HIS B 211     -26.783  21.262  41.207  1.00 26.97           N  
ANISOU 4175  ND1 HIS B 211     3132   3304   3810   -420    104   -338       N  
ATOM   4176  CD2 HIS B 211     -26.941  20.438  43.226  1.00 21.27           C  
ANISOU 4176  CD2 HIS B 211     2443   2510   3127   -422    189   -297       C  
ATOM   4177  CE1 HIS B 211     -28.041  20.883  41.376  1.00 27.59           C  
ANISOU 4177  CE1 HIS B 211     3165   3384   3934   -442    127   -362       C  
ATOM   4178  NE2 HIS B 211     -28.168  20.386  42.595  1.00 25.51           N  
ANISOU 4178  NE2 HIS B 211     2922   3074   3697   -445    181   -337       N  
ATOM   4179  N   PHE B 212     -21.394  19.802  41.685  1.00 26.21           N  
ANISOU 4179  N   PHE B 212     3216   3106   3635   -383    116   -258       N  
ATOM   4180  CA  PHE B 212     -20.007  20.123  41.391  1.00 24.16           C  
ANISOU 4180  CA  PHE B 212     2989   2851   3339   -363     91   -241       C  
ATOM   4181  C   PHE B 212     -19.301  19.012  40.616  1.00 27.08           C  
ANISOU 4181  C   PHE B 212     3365   3202   3723   -381     98   -262       C  
ATOM   4182  O   PHE B 212     -18.835  19.213  39.485  1.00 26.32           O  
ANISOU 4182  O   PHE B 212     3264   3130   3607   -382     66   -282       O  
ATOM   4183  CB  PHE B 212     -19.325  20.460  42.724  1.00 22.65           C  
ANISOU 4183  CB  PHE B 212     2836   2641   3127   -335    107   -196       C  
ATOM   4184  CG  PHE B 212     -17.877  20.756  42.601  1.00 23.48           C  
ANISOU 4184  CG  PHE B 212     2972   2748   3199   -315     84   -178       C  
ATOM   4185  CD1 PHE B 212     -17.439  21.922  41.999  1.00 28.41           C  
ANISOU 4185  CD1 PHE B 212     3597   3404   3794   -302     43   -177       C  
ATOM   4186  CD2 PHE B 212     -16.937  19.850  43.079  1.00 27.62           C  
ANISOU 4186  CD2 PHE B 212     3525   3243   3727   -309    108   -159       C  
ATOM   4187  CE1 PHE B 212     -16.080  22.183  41.897  1.00 33.87           C  
ANISOU 4187  CE1 PHE B 212     4314   4095   4461   -286     26   -162       C  
ATOM   4188  CE2 PHE B 212     -15.581  20.110  42.964  1.00 34.93           C  
ANISOU 4188  CE2 PHE B 212     4475   4173   4625   -290     87   -143       C  
ATOM   4189  CZ  PHE B 212     -15.160  21.274  42.383  1.00 30.69           C  
ANISOU 4189  CZ  PHE B 212     3934   3665   4060   -281     46   -147       C  
ATOM   4190  N   ILE B 213     -19.296  17.800  41.182  1.00 24.35           N  
ANISOU 4190  N   ILE B 213     3029   2812   3412   -394    145   -259       N  
ATOM   4191  CA AILE B 213     -18.546  16.698  40.582  0.83 25.69           C  
ANISOU 4191  CA AILE B 213     3208   2954   3598   -407    160   -275       C  
ATOM   4192  CA BILE B 213     -18.539  16.706  40.576  0.17 25.73           C  
ANISOU 4192  CA BILE B 213     3213   2960   3603   -407    159   -275       C  
ATOM   4193  C   ILE B 213     -19.175  16.271  39.259  1.00 25.46           C  
ANISOU 4193  C   ILE B 213     3141   2942   3589   -440    146   -334       C  
ATOM   4194  O   ILE B 213     -18.491  16.134  38.237  1.00 27.92           O  
ANISOU 4194  O   ILE B 213     3456   3268   3885   -443    123   -356       O  
ATOM   4195  CB AILE B 213     -18.456  15.516  41.567  0.83 24.83           C  
ANISOU 4195  CB AILE B 213     3118   2789   3526   -410    221   -253       C  
ATOM   4196  CB BILE B 213     -18.405  15.528  41.559  0.17 25.02           C  
ANISOU 4196  CB BILE B 213     3144   2814   3549   -409    220   -252       C  
ATOM   4197  CG1AILE B 213     -17.430  15.789  42.652  0.83 25.95           C  
ANISOU 4197  CG1AILE B 213     3303   2922   3637   -371    227   -197       C  
ATOM   4198  CG1BILE B 213     -17.478  15.907  42.711  0.17 26.15           C  
ANISOU 4198  CG1BILE B 213     3327   2950   3659   -369    225   -195       C  
ATOM   4199  CG2AILE B 213     -17.998  14.243  40.816  0.83 31.93           C  
ANISOU 4199  CG2AILE B 213     4018   3654   4458   -432    244   -282       C  
ATOM   4200  CG2BILE B 213     -17.858  14.293  40.841  0.17 31.24           C  
ANISOU 4200  CG2BILE B 213     3934   3568   4366   -428    242   -278       C  
ATOM   4201  CD1AILE B 213     -17.606  14.869  43.875  0.83 29.26           C  
ANISOU 4201  CD1AILE B 213     3739   3293   4084   -363    289   -163       C  
ATOM   4202  CD1BILE B 213     -16.074  16.241  42.266  0.17 27.93           C  
ANISOU 4202  CD1BILE B 213     3576   3190   3848   -349    191   -184       C  
ATOM   4203  N   ILE B 214     -20.489  16.046  39.253  1.00 23.71           N  
ANISOU 4203  N   ILE B 214     2882   2725   3403   -466    160   -365       N  
ATOM   4204  CA  ILE B 214     -21.137  15.563  38.033  1.00 22.56           C  
ANISOU 4204  CA  ILE B 214     2695   2600   3278   -500    146   -428       C  
ATOM   4205  C   ILE B 214     -20.991  16.561  36.884  1.00 25.66           C  
ANISOU 4205  C   ILE B 214     3075   3056   3620   -486     84   -445       C  
ATOM   4206  O   ILE B 214     -20.565  16.152  35.793  1.00 27.62           O  
ANISOU 4206  O   ILE B 214     3318   3317   3859   -497     67   -480       O  
ATOM   4207  CB  ILE B 214     -22.594  15.161  38.330  1.00 27.52           C  
ANISOU 4207  CB  ILE B 214     3280   3220   3957   -530    173   -458       C  
ATOM   4208  CG1 ILE B 214     -22.603  13.844  39.129  1.00 29.16           C  
ANISOU 4208  CG1 ILE B 214     3500   3357   4224   -550    242   -452       C  
ATOM   4209  CG2 ILE B 214     -23.395  15.042  37.006  1.00 33.10           C  
ANISOU 4209  CG2 ILE B 214     3933   3971   4671   -559    140   -529       C  
ATOM   4210  CD1 ILE B 214     -23.957  13.388  39.594  1.00 29.03           C  
ANISOU 4210  CD1 ILE B 214     3444   3322   4266   -579    282   -474       C  
ATOM   4211  N   PRO B 215     -21.259  17.865  37.061  1.00 21.45           N  
ANISOU 4211  N   PRO B 215     2537   2560   3052   -460     52   -418       N  
ATOM   4212  CA  PRO B 215     -20.994  18.810  35.962  1.00 29.73           C  
ANISOU 4212  CA  PRO B 215     3580   3665   4052   -441      0   -425       C  
ATOM   4213  C   PRO B 215     -19.566  18.748  35.456  1.00 24.07           C  
ANISOU 4213  C   PRO B 215     2898   2941   3305   -427    -11   -412       C  
ATOM   4214  O   PRO B 215     -19.342  18.729  34.242  1.00 26.87           O  
ANISOU 4214  O   PRO B 215     3243   3328   3637   -428    -38   -441       O  
ATOM   4215  CB  PRO B 215     -21.283  20.178  36.597  1.00 26.96           C  
ANISOU 4215  CB  PRO B 215     3232   3334   3676   -411    -17   -383       C  
ATOM   4216  CG  PRO B 215     -22.216  19.910  37.699  1.00 29.69           C  
ANISOU 4216  CG  PRO B 215     3565   3655   4061   -423     18   -377       C  
ATOM   4217  CD  PRO B 215     -22.039  18.488  38.149  1.00 25.99           C  
ANISOU 4217  CD  PRO B 215     3107   3132   3635   -449     65   -389       C  
ATOM   4218  N   LEU B 216     -18.589  18.691  36.370  1.00 24.18           N  
ANISOU 4218  N   LEU B 216     2953   2915   3318   -411     11   -369       N  
ATOM   4219  CA  LEU B 216     -17.194  18.666  35.958  1.00 27.66           C  
ANISOU 4219  CA  LEU B 216     3426   3350   3733   -396      2   -354       C  
ATOM   4220  C   LEU B 216     -16.887  17.412  35.153  1.00 30.44           C  
ANISOU 4220  C   LEU B 216     3775   3686   4106   -420     17   -394       C  
ATOM   4221  O   LEU B 216     -16.112  17.452  34.198  1.00 32.23           O  
ANISOU 4221  O   LEU B 216     4010   3929   4306   -413     -2   -404       O  
ATOM   4222  CB  LEU B 216     -16.297  18.747  37.193  1.00 25.21           C  
ANISOU 4222  CB  LEU B 216     3153   3003   3422   -376     23   -304       C  
ATOM   4223  CG  LEU B 216     -16.144  20.150  37.785  1.00 35.55           C  
ANISOU 4223  CG  LEU B 216     4474   4333   4701   -347      0   -267       C  
ATOM   4224  CD1 LEU B 216     -15.089  20.144  38.871  1.00 37.62           C  
ANISOU 4224  CD1 LEU B 216     4771   4566   4956   -327     16   -226       C  
ATOM   4225  CD2 LEU B 216     -15.805  21.169  36.706  1.00 34.59           C  
ANISOU 4225  CD2 LEU B 216     4346   4252   4544   -333    -40   -269       C  
ATOM   4226  N   ILE B 217     -17.467  16.281  35.545  1.00 25.58           N  
ANISOU 4226  N   ILE B 217     3149   3032   3538   -448     56   -417       N  
ATOM   4227  CA  ILE B 217     -17.248  15.039  34.813  1.00 27.95           C  
ANISOU 4227  CA  ILE B 217     3445   3310   3866   -474     77   -461       C  
ATOM   4228  C   ILE B 217     -17.739  15.176  33.381  1.00 25.25           C  
ANISOU 4228  C   ILE B 217     3070   3021   3503   -488     40   -518       C  
ATOM   4229  O   ILE B 217     -17.073  14.729  32.440  1.00 30.45           O  
ANISOU 4229  O   ILE B 217     3736   3686   4149   -492     34   -545       O  
ATOM   4230  CB  ILE B 217     -17.947  13.869  35.528  1.00 31.70           C  
ANISOU 4230  CB  ILE B 217     3910   3733   4404   -503    131   -477       C  
ATOM   4231  CG1 ILE B 217     -17.234  13.506  36.818  1.00 34.74           C  
ANISOU 4231  CG1 ILE B 217     4334   4064   4803   -484    173   -420       C  
ATOM   4232  CG2 ILE B 217     -18.007  12.633  34.633  1.00 36.04           C  
ANISOU 4232  CG2 ILE B 217     4444   4261   4988   -538    151   -539       C  
ATOM   4233  CD1 ILE B 217     -17.958  12.423  37.571  1.00 37.26           C  
ANISOU 4233  CD1 ILE B 217     4644   4328   5184   -508    232   -426       C  
ATOM   4234  N   VAL B 218     -18.919  15.789  33.198  1.00 22.97           N  
ANISOU 4234  N   VAL B 218     2743   2776   3210   -494     15   -537       N  
ATOM   4235  CA  VAL B 218     -19.478  15.977  31.863  1.00 24.17           C  
ANISOU 4235  CA  VAL B 218     2859   2989   3336   -502    -25   -590       C  
ATOM   4236  C   VAL B 218     -18.607  16.903  31.033  1.00 31.31           C  
ANISOU 4236  C   VAL B 218     3783   3936   4178   -467    -64   -567       C  
ATOM   4237  O   VAL B 218     -18.378  16.662  29.843  1.00 28.55           O  
ANISOU 4237  O   VAL B 218     3426   3620   3803   -470    -84   -606       O  
ATOM   4238  CB  VAL B 218     -20.911  16.518  31.964  1.00 29.53           C  
ANISOU 4238  CB  VAL B 218     3492   3706   4022   -509    -43   -606       C  
ATOM   4239  CG1 VAL B 218     -21.466  16.801  30.572  1.00 28.81           C  
ANISOU 4239  CG1 VAL B 218     3362   3690   3896   -509    -90   -657       C  
ATOM   4240  CG2 VAL B 218     -21.806  15.513  32.720  1.00 28.31           C  
ANISOU 4240  CG2 VAL B 218     3314   3506   3937   -547      2   -633       C  
ATOM   4241  N   ILE B 219     -18.152  18.006  31.634  1.00 28.26           N  
ANISOU 4241  N   ILE B 219     3421   3552   3766   -434    -74   -506       N  
ATOM   4242  CA  ILE B 219     -17.329  18.978  30.917  1.00 28.53           C  
ANISOU 4242  CA  ILE B 219     3472   3621   3746   -401   -106   -479       C  
ATOM   4243  C   ILE B 219     -16.028  18.330  30.445  1.00 30.65           C  
ANISOU 4243  C   ILE B 219     3771   3866   4008   -400    -93   -482       C  
ATOM   4244  O   ILE B 219     -15.626  18.475  29.282  1.00 33.21           O  
ANISOU 4244  O   ILE B 219     4095   4227   4295   -389   -114   -498       O  
ATOM   4245  CB  ILE B 219     -17.059  20.209  31.810  1.00 28.85           C  
ANISOU 4245  CB  ILE B 219     3533   3656   3774   -371   -111   -417       C  
ATOM   4246  CG1 ILE B 219     -18.334  21.062  31.950  1.00 25.19           C  
ANISOU 4246  CG1 ILE B 219     3036   3229   3306   -364   -130   -416       C  
ATOM   4247  CG2 ILE B 219     -15.950  21.040  31.211  1.00 31.27           C  
ANISOU 4247  CG2 ILE B 219     3863   3979   4038   -340   -129   -386       C  
ATOM   4248  CD1 ILE B 219     -18.326  22.024  33.172  1.00 31.32           C  
ANISOU 4248  CD1 ILE B 219     3829   3984   4086   -344   -122   -364       C  
ATOM   4249  N   PHE B 220     -15.350  17.603  31.338  1.00 28.08           N  
ANISOU 4249  N   PHE B 220     3472   3481   3715   -407    -56   -463       N  
ATOM   4250  CA  PHE B 220     -14.063  17.040  30.950  1.00 31.06           C  
ANISOU 4250  CA  PHE B 220     3878   3835   4087   -402    -43   -460       C  
ATOM   4251  C   PHE B 220     -14.225  15.842  30.023  1.00 30.63           C  
ANISOU 4251  C   PHE B 220     3811   3778   4049   -430    -31   -522       C  
ATOM   4252  O   PHE B 220     -13.340  15.575  29.204  1.00 33.82           O  
ANISOU 4252  O   PHE B 220     4230   4187   4433   -423    -32   -533       O  
ATOM   4253  CB  PHE B 220     -13.240  16.726  32.191  1.00 34.28           C  
ANISOU 4253  CB  PHE B 220     4318   4186   4521   -394    -10   -415       C  
ATOM   4254  CG  PHE B 220     -12.609  17.961  32.769  1.00 47.66           C  
ANISOU 4254  CG  PHE B 220     6030   5890   6187   -362    -28   -360       C  
ATOM   4255  CD1 PHE B 220     -11.551  18.581  32.115  1.00 48.38           C  
ANISOU 4255  CD1 PHE B 220     6136   5999   6246   -341    -46   -342       C  
ATOM   4256  CD2 PHE B 220     -13.118  18.553  33.907  1.00 43.83           C  
ANISOU 4256  CD2 PHE B 220     5544   5398   5710   -356    -27   -330       C  
ATOM   4257  CE1 PHE B 220     -10.986  19.744  32.619  1.00 50.21           C  
ANISOU 4257  CE1 PHE B 220     6381   6238   6459   -315    -61   -297       C  
ATOM   4258  CE2 PHE B 220     -12.552  19.713  34.420  1.00 49.90           C  
ANISOU 4258  CE2 PHE B 220     6329   6176   6456   -329    -43   -288       C  
ATOM   4259  CZ  PHE B 220     -11.492  20.310  33.769  1.00 51.20           C  
ANISOU 4259  CZ  PHE B 220     6507   6355   6594   -311    -60   -273       C  
ATOM   4260  N   PHE B 221     -15.349  15.131  30.103  1.00 32.76           N  
ANISOU 4260  N   PHE B 221     4051   4042   4355   -462    -18   -568       N  
ATOM   4261  CA  PHE B 221     -15.620  14.102  29.107  1.00 38.72           C  
ANISOU 4261  CA  PHE B 221     4786   4803   5123   -492    -12   -640       C  
ATOM   4262  C   PHE B 221     -15.749  14.724  27.720  1.00 34.28           C  
ANISOU 4262  C   PHE B 221     4207   4316   4502   -479    -58   -670       C  
ATOM   4263  O   PHE B 221     -15.094  14.291  26.762  1.00 34.19           O  
ANISOU 4263  O   PHE B 221     4205   4316   4471   -478    -60   -699       O  
ATOM   4264  CB  PHE B 221     -16.890  13.336  29.479  1.00 33.14           C  
ANISOU 4264  CB  PHE B 221     4044   4078   4470   -531     10   -685       C  
ATOM   4265  CG  PHE B 221     -17.317  12.338  28.438  1.00 40.78           C  
ANISOU 4265  CG  PHE B 221     4984   5056   5454   -566     13   -770       C  
ATOM   4266  CD1 PHE B 221     -18.121  12.719  27.372  1.00 38.49           C  
ANISOU 4266  CD1 PHE B 221     4655   4841   5130   -571    -32   -822       C  
ATOM   4267  CD2 PHE B 221     -16.912  11.018  28.522  1.00 47.98           C  
ANISOU 4267  CD2 PHE B 221     5908   5905   6417   -592     62   -799       C  
ATOM   4268  CE1 PHE B 221     -18.502  11.804  26.402  1.00 48.71           C  
ANISOU 4268  CE1 PHE B 221     5921   6151   6436   -604    -32   -908       C  
ATOM   4269  CE2 PHE B 221     -17.299  10.093  27.560  1.00 52.02           C  
ANISOU 4269  CE2 PHE B 221     6394   6424   6947   -627     66   -885       C  
ATOM   4270  CZ  PHE B 221     -18.095  10.490  26.502  1.00 47.47           C  
ANISOU 4270  CZ  PHE B 221     5777   5927   6333   -634     18   -942       C  
ATOM   4271  N   CYS B 222     -16.577  15.765  27.604  1.00 28.93           N  
ANISOU 4271  N   CYS B 222     3504   3693   3795   -464    -95   -660       N  
ATOM   4272  CA  CYS B 222     -16.777  16.424  26.314  1.00 41.70           C  
ANISOU 4272  CA  CYS B 222     5103   5388   5352   -445   -140   -681       C  
ATOM   4273  C   CYS B 222     -15.472  16.985  25.777  1.00 36.52           C  
ANISOU 4273  C   CYS B 222     4484   4741   4650   -410   -146   -641       C  
ATOM   4274  O   CYS B 222     -15.184  16.880  24.574  1.00 40.80           O  
ANISOU 4274  O   CYS B 222     5025   5325   5152   -401   -163   -671       O  
ATOM   4275  CB  CYS B 222     -17.823  17.530  26.450  1.00 32.50           C  
ANISOU 4275  CB  CYS B 222     3908   4272   4167   -428   -173   -662       C  
ATOM   4276  SG  CYS B 222     -19.481  16.924  26.709  1.00 36.54           S  
ANISOU 4276  SG  CYS B 222     4363   4795   4725   -468   -173   -723       S  
ATOM   4277  N   TYR B 223     -14.655  17.559  26.658  1.00 35.71           N  
ANISOU 4277  N   TYR B 223     4415   4600   4555   -390   -132   -574       N  
ATOM   4278  CA  TYR B 223     -13.366  18.096  26.253  1.00 44.42           C  
ANISOU 4278  CA  TYR B 223     5550   5704   5624   -359   -134   -534       C  
ATOM   4279  C   TYR B 223     -12.422  16.990  25.807  1.00 46.95           C  
ANISOU 4279  C   TYR B 223     5890   5993   5954   -371   -108   -561       C  
ATOM   4280  O   TYR B 223     -11.698  17.153  24.822  1.00 43.16           O  
ANISOU 4280  O   TYR B 223     5422   5540   5436   -353   -116   -563       O  
ATOM   4281  CB  TYR B 223     -12.757  18.892  27.412  1.00 48.32           C  
ANISOU 4281  CB  TYR B 223     6068   6161   6130   -340   -124   -466       C  
ATOM   4282  CG  TYR B 223     -11.233  18.876  27.492  1.00 61.18           C  
ANISOU 4282  CG  TYR B 223     7732   7757   7756   -325   -107   -431       C  
ATOM   4283  CD1 TYR B 223     -10.471  19.828  26.825  1.00 63.86           C  
ANISOU 4283  CD1 TYR B 223     8084   8124   8056   -294   -121   -399       C  
ATOM   4284  CD2 TYR B 223     -10.566  17.927  28.266  1.00 58.57           C  
ANISOU 4284  CD2 TYR B 223     7420   7368   7465   -338    -73   -427       C  
ATOM   4285  CE1 TYR B 223      -9.085  19.826  26.909  1.00 59.69           C  
ANISOU 4285  CE1 TYR B 223     7582   7566   7530   -281   -104   -369       C  
ATOM   4286  CE2 TYR B 223      -9.189  17.915  28.354  1.00 61.71           C  
ANISOU 4286  CE2 TYR B 223     7844   7740   7861   -322    -59   -395       C  
ATOM   4287  CZ  TYR B 223      -8.451  18.865  27.671  1.00 72.93           C  
ANISOU 4287  CZ  TYR B 223     9274   9189   9245   -295    -75   -369       C  
ATOM   4288  OH  TYR B 223      -7.076  18.851  27.758  1.00 78.59           O  
ANISOU 4288  OH  TYR B 223    10013   9881   9965   -281    -60   -340       O  
ATOM   4289  N   GLY B 224     -12.402  15.870  26.534  1.00 41.56           N  
ANISOU 4289  N   GLY B 224     5212   5253   5326   -399    -73   -579       N  
ATOM   4290  CA  GLY B 224     -11.521  14.775  26.161  1.00 41.89           C  
ANISOU 4290  CA  GLY B 224     5273   5259   5384   -410    -43   -603       C  
ATOM   4291  C   GLY B 224     -11.868  14.205  24.803  1.00 45.23           C  
ANISOU 4291  C   GLY B 224     5678   5723   5784   -424    -54   -675       C  
ATOM   4292  O   GLY B 224     -10.979  13.868  24.011  1.00 47.67           O  
ANISOU 4292  O   GLY B 224     6005   6035   6073   -415    -46   -687       O  
ATOM   4293  N   GLN B 225     -13.167  14.093  24.520  1.00 42.61           N  
ANISOU 4293  N   GLN B 225     5309   5427   5454   -446    -74   -726       N  
ATOM   4294  CA  GLN B 225     -13.619  13.710  23.192  1.00 42.05           C  
ANISOU 4294  CA  GLN B 225     5214   5412   5351   -456    -94   -799       C  
ATOM   4295  C   GLN B 225     -13.118  14.683  22.137  1.00 50.30           C  
ANISOU 4295  C   GLN B 225     6269   6524   6320   -415   -128   -777       C  
ATOM   4296  O   GLN B 225     -12.759  14.271  21.030  1.00 50.02           O  
ANISOU 4296  O   GLN B 225     6236   6519   6251   -412   -132   -820       O  
ATOM   4297  CB  GLN B 225     -15.149  13.630  23.159  1.00 41.01           C  
ANISOU 4297  CB  GLN B 225     5034   5316   5233   -483   -116   -850       C  
ATOM   4298  CG  GLN B 225     -15.736  12.482  23.955  1.00 46.53           C  
ANISOU 4298  CG  GLN B 225     5718   5951   6010   -529    -77   -889       C  
ATOM   4299  CD  GLN B 225     -15.319  11.127  23.421  1.00 53.71           C  
ANISOU 4299  CD  GLN B 225     6634   6825   6950   -559    -44   -953       C  
ATOM   4300  OE1 GLN B 225     -14.657  10.352  24.112  1.00 61.55           O  
ANISOU 4300  OE1 GLN B 225     7654   7739   7994   -569      5   -935       O  
ATOM   4301  NE2 GLN B 225     -15.702  10.833  22.183  1.00 57.07           N  
ANISOU 4301  NE2 GLN B 225     7034   7307   7343   -570    -68  -1030       N  
ATOM   4302  N   LEU B 226     -13.092  15.980  22.454  1.00 45.01           N  
ANISOU 4302  N   LEU B 226     5603   5876   5621   -382   -150   -711       N  
ATOM   4303  CA  LEU B 226     -12.639  16.967  21.475  1.00 53.07           C  
ANISOU 4303  CA  LEU B 226     6634   6957   6573   -340   -176   -683       C  
ATOM   4304  C   LEU B 226     -11.142  16.851  21.218  1.00 57.37           C  
ANISOU 4304  C   LEU B 226     7218   7472   7109   -323   -150   -653       C  
ATOM   4305  O   LEU B 226     -10.684  17.060  20.088  1.00 59.62           O  
ANISOU 4305  O   LEU B 226     7510   7801   7341   -299   -159   -660       O  
ATOM   4306  CB  LEU B 226     -12.974  18.383  21.950  1.00 59.50           C  
ANISOU 4306  CB  LEU B 226     7444   7793   7370   -310   -197   -618       C  
ATOM   4307  CG  LEU B 226     -14.443  18.782  22.011  1.00 59.39           C  
ANISOU 4307  CG  LEU B 226     7389   7825   7351   -314   -228   -638       C  
ATOM   4308  CD1 LEU B 226     -14.583  20.199  22.542  1.00 58.35           C  
ANISOU 4308  CD1 LEU B 226     7260   7703   7207   -281   -241   -567       C  
ATOM   4309  CD2 LEU B 226     -15.062  18.675  20.643  1.00 59.66           C  
ANISOU 4309  CD2 LEU B 226     7396   7943   7331   -306   -261   -694       C  
ATOM   4310  N   VAL B 227     -10.361  16.532  22.251  1.00 49.76           N  
ANISOU 4310  N   VAL B 227     6277   6434   6194   -331   -117   -618       N  
ATOM   4311  CA  VAL B 227      -8.909  16.539  22.108  1.00 54.07           C  
ANISOU 4311  CA  VAL B 227     6857   6952   6734   -312    -94   -583       C  
ATOM   4312  C   VAL B 227      -8.427  15.305  21.361  1.00 60.42           C  
ANISOU 4312  C   VAL B 227     7670   7744   7544   -327    -71   -638       C  
ATOM   4313  O   VAL B 227      -7.700  15.409  20.367  1.00 67.64           O  
ANISOU 4313  O   VAL B 227     8598   8685   8418   -306    -70   -640       O  
ATOM   4314  CB  VAL B 227      -8.237  16.659  23.484  1.00 57.66           C  
ANISOU 4314  CB  VAL B 227     7330   7341   7236   -312    -72   -527       C  
ATOM   4315  CG1 VAL B 227      -6.789  16.200  23.405  1.00 58.63           C  
ANISOU 4315  CG1 VAL B 227     7481   7426   7370   -302    -42   -508       C  
ATOM   4316  CG2 VAL B 227      -8.317  18.092  23.962  1.00 55.07           C  
ANISOU 4316  CG2 VAL B 227     7002   7030   6891   -287    -93   -467       C  
ATOM   4317  N   PHE B 228      -8.826  14.124  21.818  1.00 54.16           N  
ANISOU 4317  N   PHE B 228     6869   6907   6802   -364    -48   -684       N  
ATOM   4318  CA  PHE B 228      -8.417  12.875  21.178  1.00 64.63           C  
ANISOU 4318  CA  PHE B 228     8202   8211   8142   -382    -20   -741       C  
ATOM   4319  C   PHE B 228      -9.368  12.472  20.051  1.00 73.41           C  
ANISOU 4319  C   PHE B 228     9287   9382   9224   -399    -42   -825       C  
ATOM   4320  O   PHE B 228      -9.854  11.343  20.006  1.00 88.85           O  
ANISOU 4320  O   PHE B 228    11229  11312  11219   -436    -23   -892       O  
ATOM   4321  CB  PHE B 228      -8.314  11.774  22.226  1.00 62.39           C  
ANISOU 4321  CB  PHE B 228     7926   7845   7934   -410     24   -746       C  
ATOM   4322  N   THR B 229      -9.632  13.395  19.126  1.00 75.73           N  
ANISOU 4322  N   THR B 229     9572   9756   9448   -372    -81   -823       N  
ATOM   4323  CA  THR B 229     -10.489  13.149  17.960  1.00 78.22           C  
ANISOU 4323  CA  THR B 229     9858  10144   9718   -380   -110   -900       C  
ATOM   4324  C   THR B 229     -10.559  14.401  17.093  1.00 84.53           C  
ANISOU 4324  C   THR B 229    10654  11028  10434   -334   -150   -868       C  
ATOM   4325  O   THR B 229     -11.567  15.111  17.098  1.00 82.34           O  
ANISOU 4325  O   THR B 229    10349  10803  10134   -326   -186   -864       O  
ATOM   4326  CB  THR B 229     -11.932  12.738  18.347  1.00 73.46           C  
ANISOU 4326  CB  THR B 229     9212   9548   9150   -418   -126   -956       C  
ATOM   4327  N   GLN B 244     -15.465  26.861  10.372  1.00 68.60           N  
ANISOU 4327  N   GLN B 244     8525   9824   7717    241   -446   -394       N  
ATOM   4328  CA  GLN B 244     -14.190  26.275  10.781  1.00 74.79           C  
ANISOU 4328  CA  GLN B 244     9350  10518   8550    202   -402   -397       C  
ATOM   4329  C   GLN B 244     -13.418  27.233  11.678  1.00 73.61           C  
ANISOU 4329  C   GLN B 244     9230  10278   8458    208   -360   -307       C  
ATOM   4330  O   GLN B 244     -13.202  26.953  12.854  1.00 60.49           O  
ANISOU 4330  O   GLN B 244     7574   8532   6877    159   -344   -312       O  
ATOM   4331  CB  GLN B 244     -13.342  25.910   9.562  1.00 72.81           C  
ANISOU 4331  CB  GLN B 244     9125  10309   8231    229   -389   -410       C  
ATOM   4332  N   LYS B 245     -12.982  28.356  11.101  1.00 68.70           N  
ANISOU 4332  N   LYS B 245     8631   9677   7796    270   -339   -226       N  
ATOM   4333  CA  LYS B 245     -12.348  29.401  11.897  1.00 65.93           C  
ANISOU 4333  CA  LYS B 245     8304   9246   7500    278   -299   -142       C  
ATOM   4334  C   LYS B 245     -13.347  30.018  12.867  1.00 61.43           C  
ANISOU 4334  C   LYS B 245     7708   8658   6975    272   -316   -124       C  
ATOM   4335  O   LYS B 245     -12.993  30.368  14.003  1.00 47.87           O  
ANISOU 4335  O   LYS B 245     6002   6856   5331    244   -292    -96       O  
ATOM   4336  CB  LYS B 245     -11.753  30.466  10.974  1.00 73.50           C  
ANISOU 4336  CB  LYS B 245     9288  10232   8406    348   -270    -61       C  
ATOM   4337  CG  LYS B 245     -10.936  31.539  11.667  1.00 73.17           C  
ANISOU 4337  CG  LYS B 245     9273  10105   8424    356   -221     22       C  
ATOM   4338  CD  LYS B 245     -10.157  32.362  10.650  1.00 78.91           C  
ANISOU 4338  CD  LYS B 245    10028  10852   9101    418   -182     94       C  
ATOM   4339  N   ALA B 246     -14.602  30.154  12.431  1.00 55.96           N  
ANISOU 4339  N   ALA B 246     6978   8049   6237    298   -358   -143       N  
ATOM   4340  CA  ALA B 246     -15.652  30.630  13.321  1.00 53.19           C  
ANISOU 4340  CA  ALA B 246     6596   7686   5926    290   -376   -134       C  
ATOM   4341  C   ALA B 246     -15.865  29.665  14.476  1.00 43.61           C  
ANISOU 4341  C   ALA B 246     5370   6411   4787    215   -383   -197       C  
ATOM   4342  O   ALA B 246     -16.026  30.089  15.626  1.00 48.17           O  
ANISOU 4342  O   ALA B 246     5948   6925   5429    194   -370   -172       O  
ATOM   4343  CB  ALA B 246     -16.952  30.827  12.542  1.00 58.06           C  
ANISOU 4343  CB  ALA B 246     7170   8414   6477    333   -424   -150       C  
ATOM   4344  N   GLU B 247     -15.866  28.362  14.193  1.00 48.11           N  
ANISOU 4344  N   GLU B 247     5931   6998   5350    174   -399   -279       N  
ATOM   4345  CA  GLU B 247     -16.062  27.402  15.268  1.00 47.17           C  
ANISOU 4345  CA  GLU B 247     5801   6817   5303    106   -399   -335       C  
ATOM   4346  C   GLU B 247     -14.860  27.371  16.198  1.00 41.82           C  
ANISOU 4346  C   GLU B 247     5164   6036   4689     76   -354   -303       C  
ATOM   4347  O   GLU B 247     -15.020  27.253  17.415  1.00 33.06           O  
ANISOU 4347  O   GLU B 247     4052   4863   3646     39   -345   -304       O  
ATOM   4348  CB  GLU B 247     -16.354  26.010  14.703  1.00 45.19           C  
ANISOU 4348  CB  GLU B 247     5530   6606   5034     69   -422   -432       C  
ATOM   4349  CG  GLU B 247     -17.690  25.902  13.954  1.00 53.00           C  
ANISOU 4349  CG  GLU B 247     6468   7700   5971     87   -472   -481       C  
ATOM   4350  CD  GLU B 247     -18.925  26.129  14.830  1.00 49.63           C  
ANISOU 4350  CD  GLU B 247     5998   7270   5588     70   -492   -488       C  
ATOM   4351  OE1 GLU B 247     -18.810  26.573  15.996  1.00 50.24           O  
ANISOU 4351  OE1 GLU B 247     6089   7270   5729     54   -468   -444       O  
ATOM   4352  OE2 GLU B 247     -20.038  25.856  14.342  1.00 54.74           O  
ANISOU 4352  OE2 GLU B 247     6596   7996   6205     72   -534   -541       O  
ATOM   4353  N   LYS B 248     -13.650  27.503  15.650  1.00 37.84           N  
ANISOU 4353  N   LYS B 248     4697   5516   4164     95   -326   -272       N  
ATOM   4354  CA  LYS B 248     -12.460  27.528  16.498  1.00 38.75           C  
ANISOU 4354  CA  LYS B 248     4846   5538   4338     71   -287   -241       C  
ATOM   4355  C   LYS B 248     -12.517  28.678  17.511  1.00 31.22           C  
ANISOU 4355  C   LYS B 248     3897   4535   3430     80   -272   -177       C  
ATOM   4356  O   LYS B 248     -12.088  28.524  18.663  1.00 32.15           O  
ANISOU 4356  O   LYS B 248     4025   4578   3611     44   -254   -174       O  
ATOM   4357  CB  LYS B 248     -11.213  27.638  15.611  1.00 45.69           C  
ANISOU 4357  CB  LYS B 248     5758   6419   5182     98   -258   -213       C  
ATOM   4358  CG  LYS B 248      -9.897  27.405  16.308  1.00 53.42           C  
ANISOU 4358  CG  LYS B 248     6768   7312   6217     70   -220   -195       C  
ATOM   4359  CD  LYS B 248      -8.743  27.636  15.331  1.00 53.82           C  
ANISOU 4359  CD  LYS B 248     6846   7372   6232    102   -191   -163       C  
ATOM   4360  CE  LYS B 248      -8.764  29.071  14.807  1.00 64.95           C  
ANISOU 4360  CE  LYS B 248     8262   8807   7608    160   -179    -88       C  
ATOM   4361  NZ  LYS B 248      -7.626  29.378  13.892  1.00 65.46           N  
ANISOU 4361  NZ  LYS B 248     8354   8876   7641    193   -143    -48       N  
ATOM   4362  N   GLU B 249     -13.019  29.841  17.096  1.00 32.36           N  
ANISOU 4362  N   GLU B 249     4034   4719   3542    130   -277   -126       N  
ATOM   4363  CA  GLU B 249     -13.096  30.984  18.006  1.00 30.03           C  
ANISOU 4363  CA  GLU B 249     3744   4376   3292    140   -260    -68       C  
ATOM   4364  C   GLU B 249     -14.027  30.686  19.177  1.00 30.45           C  
ANISOU 4364  C   GLU B 249     3772   4403   3393    102   -278   -100       C  
ATOM   4365  O   GLU B 249     -13.715  31.012  20.330  1.00 31.00           O  
ANISOU 4365  O   GLU B 249     3854   4404   3521     80   -258    -80       O  
ATOM   4366  CB  GLU B 249     -13.568  32.233  17.244  1.00 37.54           C  
ANISOU 4366  CB  GLU B 249     4688   5378   4197    206   -260     -8       C  
ATOM   4367  CG  GLU B 249     -13.543  33.520  18.081  1.00 41.05           C  
ANISOU 4367  CG  GLU B 249     5140   5767   4688    221   -234     56       C  
ATOM   4368  CD  GLU B 249     -14.228  34.714  17.413  1.00 47.44           C  
ANISOU 4368  CD  GLU B 249     5940   6626   5459    287   -234    114       C  
ATOM   4369  OE1 GLU B 249     -15.319  34.543  16.829  1.00 45.57           O  
ANISOU 4369  OE1 GLU B 249     5672   6469   5174    311   -271     94       O  
ATOM   4370  OE2 GLU B 249     -13.676  35.836  17.486  1.00 36.46           O  
ANISOU 4370  OE2 GLU B 249     4569   5194   4088    316   -196    181       O  
ATOM   4371  N   VAL B 250     -15.172  30.065  18.901  1.00 28.35           N  
ANISOU 4371  N   VAL B 250     3471   4196   3106     94   -313   -151       N  
ATOM   4372  CA  VAL B 250     -16.094  29.699  19.967  1.00 36.72           C  
ANISOU 4372  CA  VAL B 250     4505   5234   4212     57   -326   -184       C  
ATOM   4373  C   VAL B 250     -15.474  28.652  20.884  1.00 31.23           C  
ANISOU 4373  C   VAL B 250     3826   4469   3572     -1   -309   -221       C  
ATOM   4374  O   VAL B 250     -15.552  28.758  22.112  1.00 26.56           O  
ANISOU 4374  O   VAL B 250     3237   3820   3033    -25   -297   -212       O  
ATOM   4375  CB  VAL B 250     -17.424  29.205  19.375  1.00 33.46           C  
ANISOU 4375  CB  VAL B 250     4046   4902   3766     59   -368   -237       C  
ATOM   4376  CG1 VAL B 250     -18.309  28.660  20.487  1.00 30.39           C  
ANISOU 4376  CG1 VAL B 250     3630   4484   3433     13   -375   -276       C  
ATOM   4377  CG2 VAL B 250     -18.127  30.356  18.633  1.00 28.87           C  
ANISOU 4377  CG2 VAL B 250     3446   4390   3134    122   -385   -191       C  
ATOM   4378  N   THR B 251     -14.881  27.603  20.305  1.00 29.98           N  
ANISOU 4378  N   THR B 251     3677   4316   3398    -21   -308   -264       N  
ATOM   4379  CA  THR B 251     -14.242  26.573  21.125  1.00 29.78           C  
ANISOU 4379  CA  THR B 251     3668   4224   3424    -70   -288   -294       C  
ATOM   4380  C   THR B 251     -13.166  27.166  22.032  1.00 26.14           C  
ANISOU 4380  C   THR B 251     3240   3690   3002    -70   -256   -241       C  
ATOM   4381  O   THR B 251     -13.033  26.777  23.204  1.00 29.35           O  
ANISOU 4381  O   THR B 251     3652   4039   3460   -103   -244   -247       O  
ATOM   4382  CB  THR B 251     -13.633  25.489  20.224  1.00 31.72           C  
ANISOU 4382  CB  THR B 251     3922   4486   3644    -82   -286   -341       C  
ATOM   4383  OG1 THR B 251     -14.654  24.941  19.369  1.00 28.73           O  
ANISOU 4383  OG1 THR B 251     3509   4179   3226    -84   -318   -399       O  
ATOM   4384  CG2 THR B 251     -13.026  24.397  21.070  1.00 32.15           C  
ANISOU 4384  CG2 THR B 251     3992   4471   3753   -129   -262   -369       C  
ATOM   4385  N   ARG B 252     -12.385  28.111  21.511  1.00 26.62           N  
ANISOU 4385  N   ARG B 252     3322   3754   3041    -34   -242   -189       N  
ATOM   4386  CA  ARG B 252     -11.338  28.710  22.330  1.00 24.47           C  
ANISOU 4386  CA  ARG B 252     3076   3414   2808    -36   -213   -144       C  
ATOM   4387  C   ARG B 252     -11.927  29.480  23.503  1.00 25.52           C  
ANISOU 4387  C   ARG B 252     3200   3516   2979    -40   -213   -120       C  
ATOM   4388  O   ARG B 252     -11.405  29.415  24.619  1.00 24.58           O  
ANISOU 4388  O   ARG B 252     3094   3339   2906    -64   -198   -115       O  
ATOM   4389  CB  ARG B 252     -10.466  29.628  21.472  1.00 25.82           C  
ANISOU 4389  CB  ARG B 252     3266   3594   2951      4   -194    -93       C  
ATOM   4390  CG  ARG B 252      -9.502  28.836  20.608  1.00 23.63           C  
ANISOU 4390  CG  ARG B 252     3005   3325   2650      2   -183   -112       C  
ATOM   4391  CD  ARG B 252      -8.925  29.720  19.546  1.00 28.63           C  
ANISOU 4391  CD  ARG B 252     3652   3984   3243     48   -166    -64       C  
ATOM   4392  NE  ARG B 252      -7.819  29.055  18.885  1.00 35.29           N  
ANISOU 4392  NE  ARG B 252     4514   4822   4072     45   -147    -75       N  
ATOM   4393  CZ  ARG B 252      -7.023  29.663  18.019  1.00 44.98           C  
ANISOU 4393  CZ  ARG B 252     5758   6059   5272     80   -122    -33       C  
ATOM   4394  NH1 ARG B 252      -7.176  30.944  17.731  1.00 44.10           N  
ANISOU 4394  NH1 ARG B 252     5649   5960   5149    120   -111     24       N  
ATOM   4395  NH2 ARG B 252      -6.054  28.968  17.432  1.00 57.05           N  
ANISOU 4395  NH2 ARG B 252     7303   7585   6789     75   -104    -48       N  
ATOM   4396  N   MET B 253     -13.009  30.222  23.268  1.00 25.44           N  
ANISOU 4396  N   MET B 253     3169   3546   2950    -14   -229   -106       N  
ATOM   4397  CA  MET B 253     -13.629  30.965  24.360  1.00 22.80           C  
ANISOU 4397  CA  MET B 253     2827   3184   2652    -16   -227    -86       C  
ATOM   4398  C   MET B 253     -14.169  30.041  25.447  1.00 25.80           C  
ANISOU 4398  C   MET B 253     3196   3538   3070    -59   -233   -128       C  
ATOM   4399  O   MET B 253     -14.042  30.336  26.641  1.00 24.39           O  
ANISOU 4399  O   MET B 253     3026   3310   2931    -74   -219   -115       O  
ATOM   4400  CB  MET B 253     -14.753  31.849  23.817  1.00 21.28           C  
ANISOU 4400  CB  MET B 253     2610   3045   2431     24   -243    -64       C  
ATOM   4401  CG  MET B 253     -15.404  32.648  24.939  1.00 23.95           C  
ANISOU 4401  CG  MET B 253     2941   3352   2808     24   -237    -43       C  
ATOM   4402  SD  MET B 253     -16.521  33.872  24.260  1.00 28.17           S  
ANISOU 4402  SD  MET B 253     3451   3943   3311     81   -248     -3       S  
ATOM   4403  CE  MET B 253     -17.577  34.096  25.722  1.00 30.33           C  
ANISOU 4403  CE  MET B 253     3705   4185   3635     60   -248    -13       C  
ATOM   4404  N   VAL B 254     -14.783  28.923  25.062  1.00 25.87           N  
ANISOU 4404  N   VAL B 254     3185   3579   3067    -80   -251   -180       N  
ATOM   4405  CA  VAL B 254     -15.335  28.021  26.070  1.00 23.66           C  
ANISOU 4405  CA  VAL B 254     2893   3271   2826   -121   -250   -218       C  
ATOM   4406  C   VAL B 254     -14.225  27.462  26.959  1.00 24.88           C  
ANISOU 4406  C   VAL B 254     3078   3360   3017   -148   -225   -216       C  
ATOM   4407  O   VAL B 254     -14.384  27.353  28.180  1.00 23.85           O  
ANISOU 4407  O   VAL B 254     2950   3188   2924   -167   -214   -214       O  
ATOM   4408  CB  VAL B 254     -16.167  26.915  25.390  1.00 25.44           C  
ANISOU 4408  CB  VAL B 254     3089   3542   3037   -141   -270   -279       C  
ATOM   4409  CG1 VAL B 254     -16.608  25.844  26.392  1.00 26.97           C  
ANISOU 4409  CG1 VAL B 254     3272   3696   3278   -186   -260   -318       C  
ATOM   4410  CG2 VAL B 254     -17.417  27.562  24.711  1.00 23.73           C  
ANISOU 4410  CG2 VAL B 254     2834   3394   2786   -112   -299   -280       C  
ATOM   4411  N   ILE B 255     -13.074  27.130  26.371  1.00 25.38           N  
ANISOU 4411  N   ILE B 255     3162   3414   3067   -146   -215   -214       N  
ATOM   4412  CA  ILE B 255     -11.929  26.677  27.160  1.00 27.59           C  
ANISOU 4412  CA  ILE B 255     3468   3636   3378   -165   -192   -207       C  
ATOM   4413  C   ILE B 255     -11.577  27.704  28.223  1.00 22.62           C  
ANISOU 4413  C   ILE B 255     2852   2969   2775   -156   -182   -165       C  
ATOM   4414  O   ILE B 255     -11.317  27.366  29.389  1.00 25.08           O  
ANISOU 4414  O   ILE B 255     3172   3239   3119   -176   -171   -166       O  
ATOM   4415  CB  ILE B 255     -10.717  26.419  26.240  1.00 27.82           C  
ANISOU 4415  CB  ILE B 255     3516   3666   3386   -156   -183   -203       C  
ATOM   4416  CG1 ILE B 255     -10.977  25.231  25.328  1.00 31.67           C  
ANISOU 4416  CG1 ILE B 255     3994   4184   3854   -169   -190   -253       C  
ATOM   4417  CG2 ILE B 255      -9.468  26.203  27.078  1.00 29.51           C  
ANISOU 4417  CG2 ILE B 255     3755   3825   3634   -168   -161   -186       C  
ATOM   4418  CD1 ILE B 255      -9.887  25.074  24.259  1.00 40.03           C  
ANISOU 4418  CD1 ILE B 255     5072   5255   4884   -154   -180   -249       C  
ATOM   4419  N   ILE B 256     -11.510  28.977  27.828  1.00 21.41           N  
ANISOU 4419  N   ILE B 256     2699   2829   2606   -126   -182   -128       N  
ATOM   4420  CA  ILE B 256     -11.126  30.008  28.789  1.00 21.15           C  
ANISOU 4420  CA  ILE B 256     2677   2757   2600   -119   -170    -94       C  
ATOM   4421  C   ILE B 256     -12.238  30.220  29.822  1.00 22.13           C  
ANISOU 4421  C   ILE B 256     2789   2876   2745   -127   -175   -100       C  
ATOM   4422  O   ILE B 256     -11.963  30.484  30.998  1.00 21.94           O  
ANISOU 4422  O   ILE B 256     2774   2813   2749   -137   -165    -92       O  
ATOM   4423  CB  ILE B 256     -10.767  31.315  28.058  1.00 27.65           C  
ANISOU 4423  CB  ILE B 256     3506   3590   3409    -84   -162    -52       C  
ATOM   4424  CG1 ILE B 256      -9.517  31.112  27.180  1.00 25.15           C  
ANISOU 4424  CG1 ILE B 256     3205   3272   3078    -78   -149    -42       C  
ATOM   4425  CG2 ILE B 256     -10.487  32.419  29.093  1.00 25.29           C  
ANISOU 4425  CG2 ILE B 256     3215   3249   3144    -81   -147    -24       C  
ATOM   4426  CD1 ILE B 256      -8.269  30.720  28.010  1.00 28.87           C  
ANISOU 4426  CD1 ILE B 256     3693   3694   3583   -101   -135    -46       C  
ATOM   4427  N   MET B 257     -13.506  30.101  29.419  1.00 21.05           N  
ANISOU 4427  N   MET B 257     2626   2779   2592   -123   -191   -116       N  
ATOM   4428  CA  MET B 257     -14.581  30.190  30.414  1.00 20.58           C  
ANISOU 4428  CA  MET B 257     2552   2713   2555   -132   -193   -124       C  
ATOM   4429  C   MET B 257     -14.471  29.095  31.472  1.00 24.90           C  
ANISOU 4429  C   MET B 257     3106   3225   3130   -167   -183   -149       C  
ATOM   4430  O   MET B 257     -14.757  29.327  32.653  1.00 19.27           O  
ANISOU 4430  O   MET B 257     2396   2485   2440   -173   -174   -143       O  
ATOM   4431  CB  MET B 257     -15.954  30.117  29.731  1.00 19.20           C  
ANISOU 4431  CB  MET B 257     2343   2592   2361   -123   -213   -142       C  
ATOM   4432  CG  MET B 257     -16.250  31.297  28.819  1.00 23.71           C  
ANISOU 4432  CG  MET B 257     2905   3200   2903    -81   -222   -108       C  
ATOM   4433  SD  MET B 257     -17.815  31.033  27.965  1.00 26.66           S  
ANISOU 4433  SD  MET B 257     3232   3648   3248    -70   -252   -136       S  
ATOM   4434  CE  MET B 257     -19.001  31.170  29.313  1.00 24.10           C  
ANISOU 4434  CE  MET B 257     2888   3304   2966    -85   -247   -143       C  
ATOM   4435  N   VAL B 258     -14.100  27.885  31.073  1.00 21.73           N  
ANISOU 4435  N   VAL B 258     2707   2824   2726   -187   -182   -178       N  
ATOM   4436  CA  VAL B 258     -13.963  26.818  32.068  1.00 19.63           C  
ANISOU 4436  CA  VAL B 258     2449   2521   2488   -215   -167   -196       C  
ATOM   4437  C   VAL B 258     -12.779  27.077  32.992  1.00 22.66           C  
ANISOU 4437  C   VAL B 258     2862   2863   2887   -213   -153   -170       C  
ATOM   4438  O   VAL B 258     -12.875  26.906  34.217  1.00 21.96           O  
ANISOU 4438  O   VAL B 258     2779   2746   2818   -222   -141   -167       O  
ATOM   4439  CB  VAL B 258     -13.838  25.454  31.372  1.00 22.26           C  
ANISOU 4439  CB  VAL B 258     2778   2859   2819   -236   -165   -234       C  
ATOM   4440  CG1 VAL B 258     -13.669  24.378  32.444  1.00 26.49           C  
ANISOU 4440  CG1 VAL B 258     3325   3352   3389   -261   -142   -245       C  
ATOM   4441  CG2 VAL B 258     -15.082  25.185  30.483  1.00 26.94           C  
ANISOU 4441  CG2 VAL B 258     3336   3500   3398   -241   -183   -268       C  
ATOM   4442  N   ILE B 259     -11.642  27.496  32.430  1.00 21.61           N  
ANISOU 4442  N   ILE B 259     2744   2727   2742   -200   -153   -153       N  
ATOM   4443  CA  ILE B 259     -10.481  27.798  33.271  1.00 20.89           C  
ANISOU 4443  CA  ILE B 259     2672   2600   2664   -198   -142   -132       C  
ATOM   4444  C   ILE B 259     -10.808  28.917  34.261  1.00 20.53           C  
ANISOU 4444  C   ILE B 259     2627   2542   2630   -189   -141   -114       C  
ATOM   4445  O   ILE B 259     -10.448  28.856  35.452  1.00 21.55           O  
ANISOU 4445  O   ILE B 259     2767   2645   2774   -195   -134   -111       O  
ATOM   4446  CB  ILE B 259      -9.284  28.164  32.377  1.00 22.94           C  
ANISOU 4446  CB  ILE B 259     2942   2860   2912   -186   -140   -117       C  
ATOM   4447  CG1 ILE B 259      -8.767  26.904  31.674  1.00 23.17           C  
ANISOU 4447  CG1 ILE B 259     2975   2892   2935   -197   -136   -138       C  
ATOM   4448  CG2 ILE B 259      -8.169  28.853  33.203  1.00 22.04           C  
ANISOU 4448  CG2 ILE B 259     2841   2716   2816   -182   -133    -96       C  
ATOM   4449  CD1 ILE B 259      -7.655  27.244  30.680  1.00 29.85           C  
ANISOU 4449  CD1 ILE B 259     3830   3744   3768   -182   -131   -123       C  
ATOM   4450  N   ALA B 260     -11.504  29.957  33.787  1.00 20.72           N  
ANISOU 4450  N   ALA B 260     2641   2587   2647   -172   -148   -102       N  
ATOM   4451  CA  ALA B 260     -11.809  31.089  34.654  1.00 20.51           C  
ANISOU 4451  CA  ALA B 260     2614   2545   2633   -162   -143    -86       C  
ATOM   4452  C   ALA B 260     -12.753  30.679  35.773  1.00 22.19           C  
ANISOU 4452  C   ALA B 260     2822   2752   2857   -174   -140   -100       C  
ATOM   4453  O   ALA B 260     -12.626  31.164  36.897  1.00 19.39           O  
ANISOU 4453  O   ALA B 260     2477   2376   2515   -174   -133    -94       O  
ATOM   4454  CB  ALA B 260     -12.406  32.241  33.826  1.00 23.75           C  
ANISOU 4454  CB  ALA B 260     3013   2978   3033   -137   -146    -66       C  
ATOM   4455  N   PHE B 261     -13.736  29.827  35.459  1.00 20.39           N  
ANISOU 4455  N   PHE B 261     2577   2544   2626   -185   -144   -119       N  
ATOM   4456  CA  PHE B 261     -14.641  29.301  36.474  1.00 22.19           C  
ANISOU 4456  CA  PHE B 261     2798   2764   2868   -198   -136   -132       C  
ATOM   4457  C   PHE B 261     -13.870  28.559  37.553  1.00 22.51           C  
ANISOU 4457  C   PHE B 261     2861   2774   2920   -210   -122   -133       C  
ATOM   4458  O   PHE B 261     -14.122  28.732  38.751  1.00 21.12           O  
ANISOU 4458  O   PHE B 261     2691   2582   2752   -210   -111   -128       O  
ATOM   4459  CB  PHE B 261     -15.669  28.361  35.829  1.00 22.55           C  
ANISOU 4459  CB  PHE B 261     2818   2834   2914   -212   -140   -158       C  
ATOM   4460  CG  PHE B 261     -16.661  27.791  36.827  1.00 20.35           C  
ANISOU 4460  CG  PHE B 261     2530   2546   2657   -227   -126   -171       C  
ATOM   4461  CD1 PHE B 261     -16.352  26.669  37.579  1.00 24.73           C  
ANISOU 4461  CD1 PHE B 261     3098   3072   3227   -246   -106   -179       C  
ATOM   4462  CD2 PHE B 261     -17.881  28.427  37.032  1.00 21.76           C  
ANISOU 4462  CD2 PHE B 261     2686   2741   2841   -219   -127   -170       C  
ATOM   4463  CE1 PHE B 261     -17.241  26.186  38.528  1.00 20.85           C  
ANISOU 4463  CE1 PHE B 261     2598   2567   2756   -257    -86   -185       C  
ATOM   4464  CE2 PHE B 261     -18.797  27.931  37.948  1.00 23.35           C  
ANISOU 4464  CE2 PHE B 261     2876   2932   3064   -233   -109   -180       C  
ATOM   4465  CZ  PHE B 261     -18.463  26.811  38.711  1.00 24.44           C  
ANISOU 4465  CZ  PHE B 261     3030   3040   3218   -252    -88   -186       C  
ATOM   4466  N   LEU B 262     -12.925  27.711  37.148  1.00 22.22           N  
ANISOU 4466  N   LEU B 262     2834   2729   2880   -219   -121   -138       N  
ATOM   4467  CA  LEU B 262     -12.161  26.971  38.148  1.00 18.47           C  
ANISOU 4467  CA  LEU B 262     2378   2226   2412   -225   -107   -135       C  
ATOM   4468  C   LEU B 262     -11.322  27.901  39.015  1.00 18.97           C  
ANISOU 4468  C   LEU B 262     2456   2277   2473   -212   -110   -118       C  
ATOM   4469  O   LEU B 262     -11.245  27.715  40.226  1.00 20.50           O  
ANISOU 4469  O   LEU B 262     2660   2458   2669   -210   -101   -114       O  
ATOM   4470  CB  LEU B 262     -11.283  25.919  37.479  1.00 19.30           C  
ANISOU 4470  CB  LEU B 262     2490   2325   2517   -233   -104   -143       C  
ATOM   4471  CG  LEU B 262     -12.065  24.829  36.742  1.00 27.99           C  
ANISOU 4471  CG  LEU B 262     3576   3433   3624   -251    -98   -169       C  
ATOM   4472  CD1 LEU B 262     -11.127  24.027  35.828  1.00 30.19           C  
ANISOU 4472  CD1 LEU B 262     3861   3708   3900   -255    -96   -179       C  
ATOM   4473  CD2 LEU B 262     -12.773  23.946  37.758  1.00 30.51           C  
ANISOU 4473  CD2 LEU B 262     3895   3733   3965   -264    -76   -175       C  
ATOM   4474  N   ILE B 263     -10.671  28.904  38.423  1.00 18.88           N  
ANISOU 4474  N   ILE B 263     2445   2270   2457   -201   -120   -109       N  
ATOM   4475  CA  ILE B 263      -9.928  29.855  39.246  1.00 20.34           C  
ANISOU 4475  CA  ILE B 263     2640   2442   2646   -193   -122   -100       C  
ATOM   4476  C   ILE B 263     -10.850  30.536  40.249  1.00 23.48           C  
ANISOU 4476  C   ILE B 263     3037   2839   3047   -188   -118   -101       C  
ATOM   4477  O   ILE B 263     -10.495  30.730  41.414  1.00 22.98           O  
ANISOU 4477  O   ILE B 263     2983   2765   2982   -185   -115   -103       O  
ATOM   4478  CB  ILE B 263      -9.236  30.900  38.354  1.00 21.12           C  
ANISOU 4478  CB  ILE B 263     2736   2541   2747   -184   -127    -90       C  
ATOM   4479  CG1 ILE B 263      -8.126  30.252  37.538  1.00 22.40           C  
ANISOU 4479  CG1 ILE B 263     2902   2703   2906   -187   -128    -88       C  
ATOM   4480  CG2 ILE B 263      -8.674  32.021  39.252  1.00 17.70           C  
ANISOU 4480  CG2 ILE B 263     2308   2092   2325   -179   -126    -89       C  
ATOM   4481  CD1 ILE B 263      -7.671  31.110  36.344  1.00 25.41           C  
ANISOU 4481  CD1 ILE B 263     3279   3089   3288   -177   -128    -75       C  
ATOM   4482  N   CYS B 264     -12.037  30.934  39.798  1.00 20.63           N  
ANISOU 4482  N   CYS B 264     2662   2490   2687   -185   -117   -101       N  
ATOM   4483  CA  CYS B 264     -12.957  31.691  40.651  1.00 16.83           C  
ANISOU 4483  CA  CYS B 264     2177   2006   2211   -178   -110   -101       C  
ATOM   4484  C   CYS B 264     -13.480  30.835  41.807  1.00 16.86           C  
ANISOU 4484  C   CYS B 264     2187   2006   2214   -184    -98   -108       C  
ATOM   4485  O   CYS B 264     -13.609  31.304  42.945  1.00 23.17           O  
ANISOU 4485  O   CYS B 264     2995   2798   3012   -178    -91   -109       O  
ATOM   4486  CB  CYS B 264     -14.110  32.175  39.760  1.00 20.12           C  
ANISOU 4486  CB  CYS B 264     2573   2443   2630   -170   -113    -97       C  
ATOM   4487  SG  CYS B 264     -15.356  33.181  40.586  1.00 23.77           S  
ANISOU 4487  SG  CYS B 264     3026   2903   3101   -157   -102    -95       S  
ATOM   4488  N   TRP B 265     -13.820  29.579  41.529  1.00 17.36           N  
ANISOU 4488  N   TRP B 265     2245   2073   2279   -197    -92   -114       N  
ATOM   4489  CA  TRP B 265     -14.618  28.810  42.478  1.00 17.01           C  
ANISOU 4489  CA  TRP B 265     2201   2023   2240   -202    -73   -117       C  
ATOM   4490  C   TRP B 265     -13.855  27.699  43.182  1.00 19.97           C  
ANISOU 4490  C   TRP B 265     2594   2383   2610   -206    -62   -112       C  
ATOM   4491  O   TRP B 265     -14.289  27.272  44.245  1.00 20.25           O  
ANISOU 4491  O   TRP B 265     2637   2411   2646   -203    -42   -108       O  
ATOM   4492  CB  TRP B 265     -15.846  28.204  41.764  1.00 18.23           C  
ANISOU 4492  CB  TRP B 265     2330   2189   2407   -215    -68   -128       C  
ATOM   4493  CG  TRP B 265     -16.890  29.235  41.450  1.00 19.93           C  
ANISOU 4493  CG  TRP B 265     2524   2422   2625   -206    -75   -129       C  
ATOM   4494  CD1 TRP B 265     -17.163  29.795  40.237  1.00 20.65           C  
ANISOU 4494  CD1 TRP B 265     2597   2535   2713   -200    -93   -130       C  
ATOM   4495  CD2 TRP B 265     -17.773  29.865  42.396  1.00 20.05           C  
ANISOU 4495  CD2 TRP B 265     2536   2435   2646   -198    -62   -125       C  
ATOM   4496  NE1 TRP B 265     -18.175  30.730  40.370  1.00 20.49           N  
ANISOU 4496  NE1 TRP B 265     2560   2526   2698   -187    -92   -125       N  
ATOM   4497  CE2 TRP B 265     -18.568  30.785  41.677  1.00 20.13           C  
ANISOU 4497  CE2 TRP B 265     2523   2464   2660   -187    -72   -123       C  
ATOM   4498  CE3 TRP B 265     -17.974  29.730  43.773  1.00 18.89           C  
ANISOU 4498  CE3 TRP B 265     2403   2274   2500   -195    -41   -121       C  
ATOM   4499  CZ2 TRP B 265     -19.539  31.575  42.296  1.00 21.51           C  
ANISOU 4499  CZ2 TRP B 265     2689   2642   2843   -174    -61   -119       C  
ATOM   4500  CZ3 TRP B 265     -18.945  30.526  44.400  1.00 21.23           C  
ANISOU 4500  CZ3 TRP B 265     2692   2573   2802   -184    -29   -119       C  
ATOM   4501  CH2 TRP B 265     -19.728  31.416  43.647  1.00 18.78           C  
ANISOU 4501  CH2 TRP B 265     2357   2279   2499   -175    -39   -119       C  
ATOM   4502  N   LEU B 266     -12.780  27.150  42.601  1.00 23.38           N  
ANISOU 4502  N   LEU B 266     3033   2810   3039   -209    -69   -111       N  
ATOM   4503  CA  LEU B 266     -12.098  26.065  43.307  1.00 20.33           C  
ANISOU 4503  CA  LEU B 266     2664   2410   2651   -207    -55   -103       C  
ATOM   4504  C   LEU B 266     -11.593  26.466  44.692  1.00 17.68           C  
ANISOU 4504  C   LEU B 266     2345   2074   2298   -189    -54    -92       C  
ATOM   4505  O   LEU B 266     -11.694  25.638  45.612  1.00 21.63           O  
ANISOU 4505  O   LEU B 266     2858   2567   2794   -183    -33    -81       O  
ATOM   4506  CB  LEU B 266     -10.942  25.509  42.468  1.00 23.19           C  
ANISOU 4506  CB  LEU B 266     3030   2768   3014   -210    -63   -103       C  
ATOM   4507  CG  LEU B 266     -11.347  24.579  41.337  1.00 30.39           C  
ANISOU 4507  CG  LEU B 266     3930   3677   3940   -228    -56   -117       C  
ATOM   4508  CD1 LEU B 266     -10.069  24.045  40.702  1.00 30.92           C  
ANISOU 4508  CD1 LEU B 266     4006   3738   4006   -226    -60   -115       C  
ATOM   4509  CD2 LEU B 266     -12.190  23.438  41.856  1.00 33.26           C  
ANISOU 4509  CD2 LEU B 266     4293   4025   4321   -238    -27   -120       C  
ATOM   4510  N   PRO B 267     -11.044  27.666  44.920  1.00 20.29           N  
ANISOU 4510  N   PRO B 267     2678   2413   2618   -180    -72    -96       N  
ATOM   4511  CA  PRO B 267     -10.620  27.985  46.285  1.00 22.64           C  
ANISOU 4511  CA  PRO B 267     2990   2716   2896   -164    -73    -93       C  
ATOM   4512  C   PRO B 267     -11.775  27.926  47.273  1.00 26.52           C  
ANISOU 4512  C   PRO B 267     3486   3208   3382   -158    -52    -90       C  
ATOM   4513  O   PRO B 267     -11.637  27.341  48.351  1.00 23.68           O  
ANISOU 4513  O   PRO B 267     3141   2851   3005   -144    -38    -78       O  
ATOM   4514  CB  PRO B 267     -10.052  29.401  46.165  1.00 26.77           C  
ANISOU 4514  CB  PRO B 267     3508   3244   3419   -162    -94   -106       C  
ATOM   4515  CG  PRO B 267      -9.661  29.533  44.700  1.00 22.97           C  
ANISOU 4515  CG  PRO B 267     3015   2758   2954   -173   -104   -106       C  
ATOM   4516  CD  PRO B 267     -10.701  28.747  43.964  1.00 21.18           C  
ANISOU 4516  CD  PRO B 267     2780   2530   2737   -183    -92   -102       C  
ATOM   4517  N   TYR B 268     -12.927  28.491  46.914  1.00 24.46           N  
ANISOU 4517  N   TYR B 268     3212   2947   3135   -166    -46    -96       N  
ATOM   4518  CA  TYR B 268     -14.094  28.416  47.796  1.00 21.97           C  
ANISOU 4518  CA  TYR B 268     2898   2632   2819   -161    -22    -93       C  
ATOM   4519  C   TYR B 268     -14.533  26.962  48.031  1.00 19.42           C  
ANISOU 4519  C   TYR B 268     2578   2298   2504   -166      6    -80       C  
ATOM   4520  O   TYR B 268     -14.796  26.550  49.171  1.00 21.21           O  
ANISOU 4520  O   TYR B 268     2818   2523   2717   -153     30    -67       O  
ATOM   4521  CB  TYR B 268     -15.246  29.232  47.198  1.00 18.95           C  
ANISOU 4521  CB  TYR B 268     2494   2252   2454   -168    -23   -102       C  
ATOM   4522  CG  TYR B 268     -16.474  29.235  48.093  1.00 18.41           C  
ANISOU 4522  CG  TYR B 268     2424   2184   2388   -162      4   -100       C  
ATOM   4523  CD1 TYR B 268     -16.541  30.082  49.186  1.00 17.65           C  
ANISOU 4523  CD1 TYR B 268     2340   2091   2274   -146      9   -102       C  
ATOM   4524  CD2 TYR B 268     -17.555  28.414  47.830  1.00 20.86           C  
ANISOU 4524  CD2 TYR B 268     2718   2490   2720   -175     25    -97       C  
ATOM   4525  CE1 TYR B 268     -17.659  30.112  50.014  1.00 21.14           C  
ANISOU 4525  CE1 TYR B 268     2780   2534   2716   -139     36    -99       C  
ATOM   4526  CE2 TYR B 268     -18.684  28.419  48.652  1.00 22.43           C  
ANISOU 4526  CE2 TYR B 268     2911   2687   2924   -170     53    -94       C  
ATOM   4527  CZ  TYR B 268     -18.711  29.260  49.756  1.00 24.91           C  
ANISOU 4527  CZ  TYR B 268     3242   3006   3217   -151     59    -93       C  
ATOM   4528  OH  TYR B 268     -19.803  29.285  50.574  1.00 22.49           O  
ANISOU 4528  OH  TYR B 268     2931   2698   2914   -144     90    -88       O  
ATOM   4529  N   ALA B 269     -14.663  26.185  46.953  1.00 19.78           N  
ANISOU 4529  N   ALA B 269     2610   2335   2571   -184      8    -84       N  
ATOM   4530  CA  ALA B 269     -15.102  24.809  47.106  1.00 22.26           C  
ANISOU 4530  CA  ALA B 269     2924   2632   2902   -192     40    -75       C  
ATOM   4531  C   ALA B 269     -14.124  24.031  47.972  1.00 19.31           C  
ANISOU 4531  C   ALA B 269     2576   2251   2512   -174     53    -54       C  
ATOM   4532  O   ALA B 269     -14.534  23.208  48.784  1.00 23.76           O  
ANISOU 4532  O   ALA B 269     3149   2801   3077   -167     88    -37       O  
ATOM   4533  CB  ALA B 269     -15.230  24.131  45.734  1.00 24.02           C  
ANISOU 4533  CB  ALA B 269     3128   2848   3151   -216     36    -91       C  
ATOM   4534  N   GLY B 270     -12.817  24.256  47.783  1.00 21.42           N  
ANISOU 4534  N   GLY B 270     2853   2526   2762   -165     27    -52       N  
ATOM   4535  CA  GLY B 270     -11.839  23.507  48.561  1.00 24.49           C  
ANISOU 4535  CA  GLY B 270     3262   2911   3132   -144     36    -31       C  
ATOM   4536  C   GLY B 270     -11.898  23.846  50.039  1.00 21.05           C  
ANISOU 4536  C   GLY B 270     2842   2491   2663   -117     44    -17       C  
ATOM   4537  O   GLY B 270     -11.865  22.960  50.895  1.00 24.54           O  
ANISOU 4537  O   GLY B 270     3301   2928   3095    -98     72      8       O  
ATOM   4538  N   VAL B 271     -11.982  25.135  50.358  1.00 17.92           N  
ANISOU 4538  N   VAL B 271     2444   2114   2250   -113     21    -34       N  
ATOM   4539  CA  VAL B 271     -12.053  25.547  51.754  1.00 19.35           C  
ANISOU 4539  CA  VAL B 271     2641   2315   2397    -88     27    -28       C  
ATOM   4540  C   VAL B 271     -13.354  25.073  52.394  1.00 23.70           C  
ANISOU 4540  C   VAL B 271     3196   2854   2953    -85     69    -13       C  
ATOM   4541  O   VAL B 271     -13.355  24.583  53.532  1.00 21.63           O  
ANISOU 4541  O   VAL B 271     2954   2601   2665    -59     92      9       O  
ATOM   4542  CB  VAL B 271     -11.884  27.072  51.849  1.00 19.87           C  
ANISOU 4542  CB  VAL B 271     2702   2398   2451    -88     -4    -56       C  
ATOM   4543  CG1 VAL B 271     -12.282  27.575  53.251  1.00 20.27           C  
ANISOU 4543  CG1 VAL B 271     2767   2468   2468    -66      6    -58       C  
ATOM   4544  CG2 VAL B 271     -10.430  27.425  51.548  1.00 22.15           C  
ANISOU 4544  CG2 VAL B 271     2987   2698   2730    -86    -39    -67       C  
ATOM   4545  N   ALA B 272     -14.471  25.169  51.661  1.00 23.24           N  
ANISOU 4545  N   ALA B 272     3119   2781   2930   -109     80    -24       N  
ATOM   4546  CA  ALA B 272     -15.743  24.649  52.168  1.00 19.37           C  
ANISOU 4546  CA  ALA B 272     2626   2278   2454   -111    123    -12       C  
ATOM   4547  C   ALA B 272     -15.652  23.164  52.462  1.00 21.72           C  
ANISOU 4547  C   ALA B 272     2935   2554   2762   -105    161     16       C  
ATOM   4548  O   ALA B 272     -16.169  22.691  53.482  1.00 24.07           O  
ANISOU 4548  O   ALA B 272     3247   2847   3051    -88    201     40       O  
ATOM   4549  CB  ALA B 272     -16.879  24.890  51.165  1.00 21.90           C  
ANISOU 4549  CB  ALA B 272     2917   2589   2816   -140    125    -31       C  
ATOM   4550  N   PHE B 273     -15.056  22.403  51.556  1.00 21.74           N  
ANISOU 4550  N   PHE B 273     2933   2541   2786   -119    156     16       N  
ATOM   4551  CA  PHE B 273     -15.001  20.971  51.786  1.00 24.79           C  
ANISOU 4551  CA  PHE B 273     3330   2900   3190   -115    198     43       C  
ATOM   4552  C   PHE B 273     -14.059  20.645  52.927  1.00 26.30           C  
ANISOU 4552  C   PHE B 273     3551   3104   3339    -74    206     76       C  
ATOM   4553  O   PHE B 273     -14.297  19.695  53.674  1.00 23.95           O  
ANISOU 4553  O   PHE B 273     3268   2789   3043    -56    252    109       O  
ATOM   4554  CB  PHE B 273     -14.586  20.231  50.517  1.00 25.41           C  
ANISOU 4554  CB  PHE B 273     3395   2956   3302   -140    192     30       C  
ATOM   4555  CG  PHE B 273     -14.695  18.728  50.649  1.00 31.13           C  
ANISOU 4555  CG  PHE B 273     4128   3644   4058   -141    244     52       C  
ATOM   4556  CD1 PHE B 273     -15.932  18.096  50.530  1.00 29.90           C  
ANISOU 4556  CD1 PHE B 273     3956   3459   3946   -165    287     46       C  
ATOM   4557  CD2 PHE B 273     -13.573  17.962  50.935  1.00 35.78           C  
ANISOU 4557  CD2 PHE B 273     4737   4224   4633   -116    253     80       C  
ATOM   4558  CE1 PHE B 273     -16.037  16.716  50.660  1.00 39.72           C  
ANISOU 4558  CE1 PHE B 273     5207   4661   5226   -168    341     66       C  
ATOM   4559  CE2 PHE B 273     -13.674  16.572  51.081  1.00 32.63           C  
ANISOU 4559  CE2 PHE B 273     4347   3784   4266   -114    307    105       C  
ATOM   4560  CZ  PHE B 273     -14.914  15.959  50.938  1.00 33.42           C  
ANISOU 4560  CZ  PHE B 273     4433   3851   4415   -141    352     97       C  
ATOM   4561  N   TYR B 274     -12.967  21.408  53.061  1.00 21.51           N  
ANISOU 4561  N   TYR B 274     2950   2528   2694    -57    161     68       N  
ATOM   4562  CA  TYR B 274     -12.096  21.215  54.214  1.00 23.76           C  
ANISOU 4562  CA  TYR B 274     3259   2837   2932    -14    161     96       C  
ATOM   4563  C   TYR B 274     -12.847  21.456  55.517  1.00 21.66           C  
ANISOU 4563  C   TYR B 274     3009   2587   2635     11    188    111       C  
ATOM   4564  O   TYR B 274     -12.760  20.652  56.459  1.00 24.92           O  
ANISOU 4564  O   TYR B 274     3443   3001   3026     44    223    150       O  
ATOM   4565  CB  TYR B 274     -10.871  22.131  54.113  1.00 24.94           C  
ANISOU 4565  CB  TYR B 274     3405   3020   3050     -6    105     74       C  
ATOM   4566  CG  TYR B 274     -10.024  22.041  55.358  1.00 29.66           C  
ANISOU 4566  CG  TYR B 274     4023   3654   3594     39     99     96       C  
ATOM   4567  CD1 TYR B 274      -9.036  21.063  55.488  1.00 33.83           C  
ANISOU 4567  CD1 TYR B 274     4559   4182   4112     65    104    126       C  
ATOM   4568  CD2 TYR B 274     -10.254  22.889  56.423  1.00 31.43           C  
ANISOU 4568  CD2 TYR B 274     4256   3911   3775     60     90     86       C  
ATOM   4569  CE1 TYR B 274      -8.283  20.985  56.652  1.00 35.62           C  
ANISOU 4569  CE1 TYR B 274     4801   4450   4283    112     96    148       C  
ATOM   4570  CE2 TYR B 274      -9.519  22.812  57.566  1.00 35.75           C  
ANISOU 4570  CE2 TYR B 274     4819   4499   4267    103     81    103       C  
ATOM   4571  CZ  TYR B 274      -8.534  21.863  57.676  1.00 35.73           C  
ANISOU 4571  CZ  TYR B 274     4823   4502   4251    130     83    134       C  
ATOM   4572  OH  TYR B 274      -7.812  21.814  58.845  1.00 45.33           O  
ANISOU 4572  OH  TYR B 274     6052   5765   5405    179     71    150       O  
ATOM   4573  N   ILE B 275     -13.646  22.525  55.577  1.00 22.45           N  
ANISOU 4573  N   ILE B 275     3099   2697   2734     -3    177     84       N  
ATOM   4574  CA  ILE B 275     -14.370  22.824  56.815  1.00 21.08           C  
ANISOU 4574  CA  ILE B 275     2941   2540   2529     21    203     96       C  
ATOM   4575  C   ILE B 275     -15.369  21.718  57.141  1.00 21.73           C  
ANISOU 4575  C   ILE B 275     3029   2591   2639     23    268    130       C  
ATOM   4576  O   ILE B 275     -15.512  21.301  58.307  1.00 24.60           O  
ANISOU 4576  O   ILE B 275     3415   2964   2970     58    303    163       O  
ATOM   4577  CB  ILE B 275     -15.069  24.189  56.690  1.00 21.06           C  
ANISOU 4577  CB  ILE B 275     2923   2548   2529      4    182     58       C  
ATOM   4578  CG1 ILE B 275     -13.991  25.294  56.636  1.00 21.06           C  
ANISOU 4578  CG1 ILE B 275     2923   2579   2500      8    125     27       C  
ATOM   4579  CG2 ILE B 275     -16.087  24.356  57.863  1.00 20.43           C  
ANISOU 4579  CG2 ILE B 275     2858   2477   2428     25    221     71       C  
ATOM   4580  CD1 ILE B 275     -14.484  26.724  56.258  1.00 27.53           C  
ANISOU 4580  CD1 ILE B 275     3726   3402   3331    -12    101    -12       C  
ATOM   4581  N   PHE B 276     -16.103  21.264  56.125  1.00 22.74           N  
ANISOU 4581  N   PHE B 276     3134   2682   2826    -16    285    119       N  
ATOM   4582  CA  PHE B 276     -17.131  20.235  56.309  1.00 22.68           C  
ANISOU 4582  CA  PHE B 276     3123   2637   2858    -24    349    144       C  
ATOM   4583  C   PHE B 276     -16.539  18.972  56.919  1.00 24.17           C  
ANISOU 4583  C   PHE B 276     3337   2810   3037      7    389    191       C  
ATOM   4584  O   PHE B 276     -17.183  18.312  57.738  1.00 23.90           O  
ANISOU 4584  O   PHE B 276     3316   2759   3008     24    448    226       O  
ATOM   4585  CB  PHE B 276     -17.779  19.923  54.952  1.00 22.13           C  
ANISOU 4585  CB  PHE B 276     3020   2535   2853    -73    350    115       C  
ATOM   4586  CG  PHE B 276     -18.841  18.827  54.982  1.00 20.95           C  
ANISOU 4586  CG  PHE B 276     2859   2343   2757    -90    415    130       C  
ATOM   4587  CD1 PHE B 276     -19.963  18.936  55.779  1.00 24.79           C  
ANISOU 4587  CD1 PHE B 276     3343   2826   3249    -85    457    142       C  
ATOM   4588  CD2 PHE B 276     -18.722  17.729  54.148  1.00 29.46           C  
ANISOU 4588  CD2 PHE B 276     3926   3383   3883   -115    434    127       C  
ATOM   4589  CE1 PHE B 276     -20.934  17.926  55.792  1.00 28.54           C  
ANISOU 4589  CE1 PHE B 276     3804   3258   3780   -104    521    153       C  
ATOM   4590  CE2 PHE B 276     -19.716  16.734  54.116  1.00 30.98           C  
ANISOU 4590  CE2 PHE B 276     4104   3532   4134   -137    496    133       C  
ATOM   4591  CZ  PHE B 276     -20.814  16.833  54.940  1.00 27.72           C  
ANISOU 4591  CZ  PHE B 276     3688   3115   3730   -132    540    147       C  
ATOM   4592  N   THR B 277     -15.324  18.614  56.504  1.00 22.47           N  
ANISOU 4592  N   THR B 277     3127   2597   2812     15    362    196       N  
ATOM   4593  CA  THR B 277     -14.633  17.427  56.984  1.00 28.08           C  
ANISOU 4593  CA  THR B 277     3861   3293   3516     48    397    242       C  
ATOM   4594  C   THR B 277     -13.795  17.698  58.229  1.00 34.26           C  
ANISOU 4594  C   THR B 277     4672   4124   4224    105    384    272       C  
ATOM   4595  O   THR B 277     -13.226  16.757  58.772  1.00 26.91           O  
ANISOU 4595  O   THR B 277     3760   3186   3276    142    414    318       O  
ATOM   4596  CB  THR B 277     -13.739  16.837  55.855  1.00 25.87           C  
ANISOU 4596  CB  THR B 277     3571   2991   3266     29    377    232       C  
ATOM   4597  OG1 THR B 277     -12.843  17.825  55.332  1.00 26.91           O  
ANISOU 4597  OG1 THR B 277     3693   3158   3371     24    308    199       O  
ATOM   4598  CG2 THR B 277     -14.582  16.351  54.678  1.00 29.61           C  
ANISOU 4598  CG2 THR B 277     4018   3418   3812    -24    398    204       C  
ATOM   4599  N   HIS B 278     -13.703  18.950  58.689  1.00 25.56           N  
ANISOU 4599  N   HIS B 278     3570   3068   3074    114    340    245       N  
ATOM   4600  CA  HIS B 278     -12.947  19.311  59.893  1.00 26.01           C  
ANISOU 4600  CA  HIS B 278     3650   3179   3055    166    321    262       C  
ATOM   4601  C   HIS B 278     -13.741  20.300  60.726  1.00 27.41           C  
ANISOU 4601  C   HIS B 278     3832   3385   3198    174    321    245       C  
ATOM   4602  O   HIS B 278     -13.249  21.366  61.096  1.00 26.47           O  
ANISOU 4602  O   HIS B 278     3714   3311   3033    185    273    214       O  
ATOM   4603  CB  HIS B 278     -11.578  19.908  59.569  1.00 27.59           C  
ANISOU 4603  CB  HIS B 278     3842   3416   3226    171    253    236       C  
ATOM   4604  CG  HIS B 278     -10.721  19.023  58.723  1.00 29.86           C  
ANISOU 4604  CG  HIS B 278     4123   3678   3545    165    250    250       C  
ATOM   4605  ND1 HIS B 278     -10.926  18.872  57.368  1.00 28.74           N  
ANISOU 4605  ND1 HIS B 278     3960   3494   3465    116    245    225       N  
ATOM   4606  CD2 HIS B 278      -9.671  18.224  59.041  1.00 33.48           C  
ANISOU 4606  CD2 HIS B 278     4593   4147   3981    204    252    286       C  
ATOM   4607  CE1 HIS B 278     -10.036  18.021  56.885  1.00 34.50           C  
ANISOU 4607  CE1 HIS B 278     4689   4208   4210    123    247    243       C  
ATOM   4608  NE2 HIS B 278      -9.262  17.617  57.876  1.00 35.01           N  
ANISOU 4608  NE2 HIS B 278     4773   4302   4226    176    251    281       N  
ATOM   4609  N   GLN B 279     -15.004  19.980  60.987  1.00 23.78           N  
ANISOU 4609  N   GLN B 279     3374   2896   2765    166    378    261       N  
ATOM   4610  CA  GLN B 279     -15.851  20.920  61.699  1.00 22.88           C  
ANISOU 4610  CA  GLN B 279     3264   2805   2626    171    382    244       C  
ATOM   4611  C   GLN B 279     -15.290  21.189  63.085  1.00 32.97           C  
ANISOU 4611  C   GLN B 279     4570   4138   3817    229    376    261       C  
ATOM   4612  O   GLN B 279     -14.830  20.273  63.774  1.00 27.24           O  
ANISOU 4612  O   GLN B 279     3867   3421   3060    273    405    311       O  
ATOM   4613  CB  GLN B 279     -17.270  20.365  61.821  1.00 27.91           C  
ANISOU 4613  CB  GLN B 279     3897   3401   3308    158    452    265       C  
ATOM   4614  CG  GLN B 279     -17.948  20.188  60.457  1.00 26.71           C  
ANISOU 4614  CG  GLN B 279     3710   3201   3237     99    454    239       C  
ATOM   4615  CD  GLN B 279     -19.383  19.778  60.615  1.00 35.98           C  
ANISOU 4615  CD  GLN B 279     4874   4341   4458     82    518    251       C  
ATOM   4616  OE1 GLN B 279     -19.776  19.229  61.654  1.00 36.03           O  
ANISOU 4616  OE1 GLN B 279     4901   4343   4446    115    576    294       O  
ATOM   4617  NE2 GLN B 279     -20.182  20.039  59.598  1.00 30.50           N  
ANISOU 4617  NE2 GLN B 279     4143   3622   3822     34    510    216       N  
ATOM   4618  N   GLY B 280     -15.319  22.458  63.490  1.00 28.71           N  
ANISOU 4618  N   GLY B 280     4030   3638   3240    231    339    219       N  
ATOM   4619  CA  GLY B 280     -14.833  22.819  64.806  1.00 31.27           C  
ANISOU 4619  CA  GLY B 280     4379   4022   3479    284    328    225       C  
ATOM   4620  C   GLY B 280     -13.327  22.951  64.917  1.00 25.63           C  
ANISOU 4620  C   GLY B 280     3667   3353   2719    307    270    213       C  
ATOM   4621  O   GLY B 280     -12.830  23.282  66.006  1.00 33.24           O  
ANISOU 4621  O   GLY B 280     4649   4376   3606    352    253    211       O  
ATOM   4622  N   SER B 281     -12.592  22.710  63.839  1.00 29.53           N  
ANISOU 4622  N   SER B 281     4142   3825   3254    279    239    204       N  
ATOM   4623  CA  SER B 281     -11.143  22.846  63.849  1.00 28.91           C  
ANISOU 4623  CA  SER B 281     4058   3787   3140    297    184    191       C  
ATOM   4624  C   SER B 281     -10.734  24.321  63.961  1.00 30.25           C  
ANISOU 4624  C   SER B 281     4215   3996   3283    284    124    124       C  
ATOM   4625  O   SER B 281     -11.551  25.256  63.885  1.00 27.75           O  
ANISOU 4625  O   SER B 281     3893   3670   2983    258    125     88       O  
ATOM   4626  CB  SER B 281     -10.537  22.199  62.602  1.00 26.77           C  
ANISOU 4626  CB  SER B 281     3769   3477   2926    268    172    198       C  
ATOM   4627  OG  SER B 281     -10.932  22.894  61.426  1.00 28.67           O  
ANISOU 4627  OG  SER B 281     3986   3683   3226    211    152    155       O  
ATOM   4628  N   ASP B 282      -9.434  24.525  64.124  1.00 30.26           N  
ANISOU 4628  N   ASP B 282     4208   4041   3248    302     73    106       N  
ATOM   4629  CA  ASP B 282      -8.903  25.835  64.496  1.00 32.79           C  
ANISOU 4629  CA  ASP B 282     4518   4407   3534    298     20     43       C  
ATOM   4630  C   ASP B 282      -8.642  26.639  63.231  1.00 35.73           C  
ANISOU 4630  C   ASP B 282     4861   4746   3970    242    -16     -4       C  
ATOM   4631  O   ASP B 282      -7.540  26.625  62.684  1.00 41.18           O  
ANISOU 4631  O   ASP B 282     5533   5444   4672    234    -54    -16       O  
ATOM   4632  CB  ASP B 282      -7.630  25.667  65.319  1.00 35.70           C  
ANISOU 4632  CB  ASP B 282     4888   4844   3833    346    -19     43       C  
ATOM   4633  CG  ASP B 282      -7.245  26.930  66.083  1.00 39.51           C  
ANISOU 4633  CG  ASP B 282     5364   5384   4265    352    -65    -23       C  
ATOM   4634  OD1 ASP B 282      -8.093  27.838  66.205  1.00 43.58           O  
ANISOU 4634  OD1 ASP B 282     5882   5886   4790    330    -55    -59       O  
ATOM   4635  OD2 ASP B 282      -6.089  27.011  66.559  1.00 50.13           O  
ANISOU 4635  OD2 ASP B 282     6697   6787   5562    379   -110    -41       O  
ATOM   4636  N   PHE B 283      -9.659  27.358  62.750  1.00 27.84           N  
ANISOU 4636  N   PHE B 283     3856   3709   3013    205     -1    -28       N  
ATOM   4637  CA  PHE B 283      -9.443  28.309  61.672  1.00 24.64           C  
ANISOU 4637  CA  PHE B 283     3425   3277   2659    158    -33    -73       C  
ATOM   4638  C   PHE B 283     -10.051  29.641  62.080  1.00 26.95           C  
ANISOU 4638  C   PHE B 283     3718   3577   2946    146    -38   -121       C  
ATOM   4639  O   PHE B 283     -10.899  29.722  62.974  1.00 26.00           O  
ANISOU 4639  O   PHE B 283     3616   3469   2795    167     -8   -116       O  
ATOM   4640  CB  PHE B 283     -10.022  27.818  60.322  1.00 24.45           C  
ANISOU 4640  CB  PHE B 283     3390   3194   2706    120    -11    -51       C  
ATOM   4641  CG  PHE B 283     -11.488  27.452  60.387  1.00 24.33           C  
ANISOU 4641  CG  PHE B 283     3385   3149   2712    116     41    -25       C  
ATOM   4642  CD1 PHE B 283     -12.461  28.417  60.169  1.00 24.75           C  
ANISOU 4642  CD1 PHE B 283     3430   3184   2790     92     49    -53       C  
ATOM   4643  CD2 PHE B 283     -11.880  26.151  60.652  1.00 27.27           C  
ANISOU 4643  CD2 PHE B 283     3771   3508   3082    135     85     27       C  
ATOM   4644  CE1 PHE B 283     -13.816  28.081  60.255  1.00 28.31           C  
ANISOU 4644  CE1 PHE B 283     3884   3609   3261     88     96    -31       C  
ATOM   4645  CE2 PHE B 283     -13.235  25.803  60.741  1.00 28.05           C  
ANISOU 4645  CE2 PHE B 283     3875   3578   3204    129    136     49       C  
ATOM   4646  CZ  PHE B 283     -14.200  26.770  60.547  1.00 29.74           C  
ANISOU 4646  CZ  PHE B 283     4079   3780   3442    105    140     18       C  
ATOM   4647  N   GLY B 284      -9.569  30.705  61.455  1.00 27.44           N  
ANISOU 4647  N   GLY B 284     3758   3630   3038    115    -73   -169       N  
ATOM   4648  CA  GLY B 284     -10.030  32.028  61.813  1.00 21.32           C  
ANISOU 4648  CA  GLY B 284     2982   2857   2263    104    -77   -219       C  
ATOM   4649  C   GLY B 284     -10.954  32.630  60.764  1.00 26.29           C  
ANISOU 4649  C   GLY B 284     3599   3432   2958     67    -59   -224       C  
ATOM   4650  O   GLY B 284     -11.284  32.011  59.744  1.00 23.82           O  
ANISOU 4650  O   GLY B 284     3278   3084   2689     48    -46   -192       O  
ATOM   4651  N   PRO B 285     -11.376  33.870  61.014  1.00 24.50           N  
ANISOU 4651  N   PRO B 285     3370   3201   2740     57    -59   -268       N  
ATOM   4652  CA  PRO B 285     -12.334  34.550  60.115  1.00 25.00           C  
ANISOU 4652  CA  PRO B 285     3421   3216   2860     29    -40   -271       C  
ATOM   4653  C   PRO B 285     -11.770  34.830  58.737  1.00 25.54           C  
ANISOU 4653  C   PRO B 285     3467   3254   2984     -3    -62   -275       C  
ATOM   4654  O   PRO B 285     -12.521  34.934  57.758  1.00 25.77           O  
ANISOU 4654  O   PRO B 285     3486   3248   3059    -22    -46   -258       O  
ATOM   4655  CB  PRO B 285     -12.639  35.869  60.858  1.00 27.07           C  
ANISOU 4655  CB  PRO B 285     3688   3485   3112     31    -38   -322       C  
ATOM   4656  CG  PRO B 285     -12.082  35.723  62.221  1.00 33.92           C  
ANISOU 4656  CG  PRO B 285     4573   4406   3910     63    -50   -342       C  
ATOM   4657  CD  PRO B 285     -11.048  34.657  62.216  1.00 28.25           C  
ANISOU 4657  CD  PRO B 285     3854   3716   3165     76    -74   -315       C  
ATOM   4658  N   ILE B 286     -10.453  35.009  58.633  1.00 21.79           N  
ANISOU 4658  N   ILE B 286     2982   2794   2503     -8    -98   -298       N  
ATOM   4659  CA  ILE B 286      -9.870  35.315  57.336  1.00 19.39           C  
ANISOU 4659  CA  ILE B 286     2657   2460   2250    -37   -114   -301       C  
ATOM   4660  C   ILE B 286      -9.917  34.120  56.404  1.00 27.92           C  
ANISOU 4660  C   ILE B 286     3734   3526   3348    -42   -107   -252       C  
ATOM   4661  O   ILE B 286      -9.951  34.287  55.173  1.00 23.58           O  
ANISOU 4661  O   ILE B 286     3170   2946   2843    -64   -108   -244       O  
ATOM   4662  CB  ILE B 286      -8.424  35.831  57.515  1.00 27.67           C  
ANISOU 4662  CB  ILE B 286     3692   3529   3293    -42   -152   -341       C  
ATOM   4663  CG1 ILE B 286      -8.439  37.125  58.327  1.00 39.43           C  
ANISOU 4663  CG1 ILE B 286     5182   5026   4775    -44   -156   -398       C  
ATOM   4664  CG2 ILE B 286      -7.784  36.117  56.162  1.00 38.72           C  
ANISOU 4664  CG2 ILE B 286     5070   4896   4745    -70   -164   -340       C  
ATOM   4665  CD1 ILE B 286      -9.366  38.177  57.767  1.00 46.78           C  
ANISOU 4665  CD1 ILE B 286     6109   5912   5754    -62   -132   -409       C  
ATOM   4666  N   PHE B 287      -9.967  32.916  56.972  1.00 22.61           N  
ANISOU 4666  N   PHE B 287     3076   2874   2641    -20    -97   -220       N  
ATOM   4667  CA  PHE B 287      -9.805  31.684  56.196  1.00 23.14           C  
ANISOU 4667  CA  PHE B 287     3142   2929   2723    -23    -91   -179       C  
ATOM   4668  C   PHE B 287     -10.839  31.579  55.073  1.00 22.19           C  
ANISOU 4668  C   PHE B 287     3011   2769   2649    -46    -69   -161       C  
ATOM   4669  O   PHE B 287     -10.497  31.304  53.908  1.00 22.20           O  
ANISOU 4669  O   PHE B 287     3000   2753   2683    -64    -77   -152       O  
ATOM   4670  CB  PHE B 287      -9.909  30.499  57.179  1.00 22.55           C  
ANISOU 4670  CB  PHE B 287     3086   2877   2604      9    -71   -145       C  
ATOM   4671  CG  PHE B 287      -9.690  29.129  56.554  1.00 25.80           C  
ANISOU 4671  CG  PHE B 287     3499   3274   3030      9    -59   -104       C  
ATOM   4672  CD1 PHE B 287      -8.553  28.853  55.816  1.00 31.79           C  
ANISOU 4672  CD1 PHE B 287     4244   4030   3802      1    -84   -104       C  
ATOM   4673  CD2 PHE B 287     -10.585  28.089  56.810  1.00 25.15           C  
ANISOU 4673  CD2 PHE B 287     3430   3179   2948     20    -18    -66       C  
ATOM   4674  CE1 PHE B 287      -8.334  27.583  55.279  1.00 34.73           C  
ANISOU 4674  CE1 PHE B 287     4619   4387   4189      3    -70    -68       C  
ATOM   4675  CE2 PHE B 287     -10.370  26.798  56.287  1.00 26.69           C  
ANISOU 4675  CE2 PHE B 287     3626   3356   3159     20     -2    -30       C  
ATOM   4676  CZ  PHE B 287      -9.247  26.547  55.519  1.00 26.67           C  
ANISOU 4676  CZ  PHE B 287     3612   3351   3170     12    -28    -32       C  
ATOM   4677  N   MET B 288     -12.119  31.807  55.387  1.00 21.30           N  
ANISOU 4677  N   MET B 288     2904   2649   2541    -44    -41   -158       N  
ATOM   4678  CA  MET B 288     -13.145  31.715  54.342  1.00 19.86           C  
ANISOU 4678  CA  MET B 288     2708   2438   2402    -64    -23   -144       C  
ATOM   4679  C   MET B 288     -13.481  33.072  53.710  1.00 20.18           C  
ANISOU 4679  C   MET B 288     2734   2463   2472    -79    -31   -168       C  
ATOM   4680  O   MET B 288     -14.040  33.100  52.605  1.00 20.53           O  
ANISOU 4680  O   MET B 288     2762   2488   2550    -95    -28   -159       O  
ATOM   4681  CB  MET B 288     -14.427  31.070  54.911  1.00 22.36           C  
ANISOU 4681  CB  MET B 288     3031   2751   2713    -55     16   -122       C  
ATOM   4682  CG  MET B 288     -15.573  30.809  53.912  1.00 24.22           C  
ANISOU 4682  CG  MET B 288     3248   2963   2992    -75     34   -109       C  
ATOM   4683  SD  MET B 288     -15.040  29.993  52.418  1.00 24.07           S  
ANISOU 4683  SD  MET B 288     3213   2929   3004    -98     19    -98       S  
ATOM   4684  CE  MET B 288     -15.873  28.386  52.483  1.00 21.69           C  
ANISOU 4684  CE  MET B 288     2911   2614   2715   -101     58    -69       C  
ATOM   4685  N   THR B 289     -13.137  34.176  54.371  1.00 20.01           N  
ANISOU 4685  N   THR B 289     2716   2448   2438    -73    -42   -200       N  
ATOM   4686  CA  THR B 289     -13.449  35.496  53.822  1.00 22.42           C  
ANISOU 4686  CA  THR B 289     3010   2733   2777    -84    -43   -221       C  
ATOM   4687  C   THR B 289     -12.852  35.683  52.438  1.00 23.76           C  
ANISOU 4687  C   THR B 289     3162   2884   2980   -103    -60   -216       C  
ATOM   4688  O   THR B 289     -13.541  36.110  51.512  1.00 22.18           O  
ANISOU 4688  O   THR B 289     2950   2666   2813   -110    -51   -206       O  
ATOM   4689  CB  THR B 289     -12.926  36.601  54.740  1.00 19.30           C  
ANISOU 4689  CB  THR B 289     2621   2345   2366    -78    -52   -263       C  
ATOM   4690  OG1 THR B 289     -13.589  36.527  55.991  1.00 21.41           O  
ANISOU 4690  OG1 THR B 289     2905   2631   2599    -59    -33   -269       O  
ATOM   4691  CG2 THR B 289     -13.188  37.992  54.111  1.00 18.70           C  
ANISOU 4691  CG2 THR B 289     2533   2239   2333    -90    -46   -283       C  
ATOM   4692  N  AILE B 290     -11.556  35.389  52.283  0.47 21.04           N  
ANISOU 4692  N  AILE B 290     2818   2548   2630   -107    -83   -221       N  
ATOM   4693  N  BILE B 290     -11.561  35.385  52.277  0.53 21.04           N  
ANISOU 4693  N  BILE B 290     2817   2547   2629   -107    -83   -221       N  
ATOM   4694  CA AILE B 290     -10.893  35.635  50.995  0.47 20.73           C  
ANISOU 4694  CA AILE B 290     2763   2491   2622   -123    -96   -217       C  
ATOM   4695  CA BILE B 290     -10.907  35.644  50.989  0.53 20.70           C  
ANISOU 4695  CA BILE B 290     2759   2487   2618   -124    -96   -217       C  
ATOM   4696  C  AILE B 290     -11.502  34.808  49.867  0.47 21.32           C  
ANISOU 4696  C  AILE B 290     2830   2558   2712   -130    -88   -185       C  
ATOM   4697  C  BILE B 290     -11.496  34.807  49.857  0.53 21.33           C  
ANISOU 4697  C  BILE B 290     2831   2559   2713   -130    -88   -185       C  
ATOM   4698  O  AILE B 290     -11.864  35.391  48.830  0.47 19.62           O  
ANISOU 4698  O  AILE B 290     2603   2328   2525   -137    -85   -179       O  
ATOM   4699  O  BILE B 290     -11.844  35.383  48.810  0.53 19.59           O  
ANISOU 4699  O  BILE B 290     2599   2324   2521   -137    -86   -178       O  
ATOM   4700  CB AILE B 290      -9.374  35.423  51.130  0.47 23.93           C  
ANISOU 4700  CB AILE B 290     3166   2909   3017   -126   -121   -230       C  
ATOM   4701  CB BILE B 290      -9.382  35.483  51.131  0.53 23.92           C  
ANISOU 4701  CB BILE B 290     3166   2907   3017   -126   -121   -231       C  
ATOM   4702  CG1AILE B 290      -8.830  36.247  52.290  0.47 24.14           C  
ANISOU 4702  CG1AILE B 290     3197   2950   3027   -120   -132   -270       C  
ATOM   4703  CG1BILE B 290      -8.882  36.423  52.225  0.53 24.29           C  
ANISOU 4703  CG1BILE B 290     3214   2964   3050   -122   -130   -272       C  
ATOM   4704  CG2AILE B 290      -8.671  35.800  49.826  0.47 26.70           C  
ANISOU 4704  CG2AILE B 290     3502   3239   3403   -142   -130   -226       C  
ATOM   4705  CG2BILE B 290      -8.693  35.752  49.794  0.53 26.67           C  
ANISOU 4705  CG2BILE B 290     3498   3235   3398   -142   -129   -224       C  
ATOM   4706  CD1AILE B 290      -9.036  37.732  52.092  0.47 27.16           C  
ANISOU 4706  CD1AILE B 290     3571   3305   3442   -131   -124   -297       C  
ATOM   4707  CD1BILE B 290      -7.423  36.327  52.507  0.53 30.06           C  
ANISOU 4707  CD1BILE B 290     3938   3713   3770   -124   -158   -292       C  
ATOM   4708  N   PRO B 291     -11.635  33.480  49.979  1.00 17.55           N  
ANISOU 4708  N   PRO B 291     2359   2091   2218   -127    -83   -164       N  
ATOM   4709  CA  PRO B 291     -12.265  32.728  48.876  1.00 19.78           C  
ANISOU 4709  CA  PRO B 291     2630   2366   2518   -137    -76   -143       C  
ATOM   4710  C   PRO B 291     -13.697  33.143  48.609  1.00 18.18           C  
ANISOU 4710  C   PRO B 291     2418   2158   2333   -138    -59   -139       C  
ATOM   4711  O   PRO B 291     -14.077  33.236  47.439  1.00 18.67           O  
ANISOU 4711  O   PRO B 291     2464   2216   2415   -146    -61   -132       O  
ATOM   4712  CB  PRO B 291     -12.213  31.261  49.332  1.00 24.76           C  
ANISOU 4712  CB  PRO B 291     3271   3004   3132   -133    -66   -126       C  
ATOM   4713  CG  PRO B 291     -11.305  31.221  50.508  1.00 25.15           C  
ANISOU 4713  CG  PRO B 291     3336   3069   3151   -117    -74   -133       C  
ATOM   4714  CD  PRO B 291     -11.184  32.590  51.079  1.00 22.17           C  
ANISOU 4714  CD  PRO B 291     2959   2695   2768   -113    -83   -160       C  
ATOM   4715  N   ALA B 292     -14.485  33.433  49.656  1.00 19.15           N  
ANISOU 4715  N   ALA B 292     2547   2284   2445   -127    -42   -145       N  
ATOM   4716  CA  ALA B 292     -15.911  33.711  49.442  1.00 20.97           C  
ANISOU 4716  CA  ALA B 292     2764   2511   2692   -126    -23   -139       C  
ATOM   4717  C   ALA B 292     -16.078  35.043  48.733  1.00 18.39           C  
ANISOU 4717  C   ALA B 292     2424   2174   2388   -125    -29   -146       C  
ATOM   4718  O   ALA B 292     -16.936  35.177  47.854  1.00 18.99           O  
ANISOU 4718  O   ALA B 292     2481   2250   2483   -126    -26   -135       O  
ATOM   4719  CB  ALA B 292     -16.697  33.679  50.785  1.00 17.89           C  
ANISOU 4719  CB  ALA B 292     2385   2126   2286   -113      1   -142       C  
ATOM   4720  N   PHE B 293     -15.235  36.036  49.069  1.00 18.80           N  
ANISOU 4720  N   PHE B 293     2486   2218   2439   -122    -38   -164       N  
ATOM   4721  CA  PHE B 293     -15.307  37.314  48.371  1.00 20.07           C  
ANISOU 4721  CA  PHE B 293     2636   2362   2627   -119    -37   -166       C  
ATOM   4722  C   PHE B 293     -14.639  37.274  47.007  1.00 19.73           C  
ANISOU 4722  C   PHE B 293     2584   2315   2599   -127    -52   -153       C  
ATOM   4723  O   PHE B 293     -15.106  37.950  46.092  1.00 21.06           O  
ANISOU 4723  O   PHE B 293     2739   2476   2787   -121    -47   -140       O  
ATOM   4724  CB  PHE B 293     -14.737  38.435  49.254  1.00 18.02           C  
ANISOU 4724  CB  PHE B 293     2388   2089   2369   -116    -34   -195       C  
ATOM   4725  CG  PHE B 293     -15.798  38.998  50.188  1.00 21.40           C  
ANISOU 4725  CG  PHE B 293     2821   2516   2795   -103    -12   -206       C  
ATOM   4726  CD1 PHE B 293     -16.227  38.251  51.279  1.00 20.29           C  
ANISOU 4726  CD1 PHE B 293     2691   2393   2624    -96     -3   -209       C  
ATOM   4727  CD2 PHE B 293     -16.418  40.219  49.925  1.00 22.38           C  
ANISOU 4727  CD2 PHE B 293     2937   2619   2948    -94      5   -208       C  
ATOM   4728  CE1 PHE B 293     -17.239  38.714  52.133  1.00 21.83           C  
ANISOU 4728  CE1 PHE B 293     2890   2587   2816    -83     21   -217       C  
ATOM   4729  CE2 PHE B 293     -17.425  40.710  50.773  1.00 21.25           C  
ANISOU 4729  CE2 PHE B 293     2797   2473   2804    -81     29   -217       C  
ATOM   4730  CZ  PHE B 293     -17.839  39.969  51.880  1.00 21.64           C  
ANISOU 4730  CZ  PHE B 293     2858   2542   2822    -76     37   -223       C  
ATOM   4731  N   PHE B 294     -13.555  36.509  46.847  1.00 19.17           N  
ANISOU 4731  N   PHE B 294     2519   2250   2517   -137    -68   -153       N  
ATOM   4732  CA  PHE B 294     -12.965  36.351  45.517  1.00 18.82           C  
ANISOU 4732  CA  PHE B 294     2465   2204   2483   -143    -79   -139       C  
ATOM   4733  C   PHE B 294     -13.974  35.738  44.552  1.00 21.46           C  
ANISOU 4733  C   PHE B 294     2785   2550   2819   -142    -77   -121       C  
ATOM   4734  O   PHE B 294     -14.059  36.145  43.376  1.00 21.60           O  
ANISOU 4734  O   PHE B 294     2791   2569   2847   -138    -80   -107       O  
ATOM   4735  CB  PHE B 294     -11.708  35.488  45.608  1.00 20.59           C  
ANISOU 4735  CB  PHE B 294     2697   2433   2694   -152    -94   -143       C  
ATOM   4736  CG  PHE B 294     -11.010  35.284  44.276  1.00 21.88           C  
ANISOU 4736  CG  PHE B 294     2852   2594   2866   -158   -103   -130       C  
ATOM   4737  CD1 PHE B 294     -10.511  36.362  43.562  1.00 26.39           C  
ANISOU 4737  CD1 PHE B 294     3418   3150   3459   -157   -101   -128       C  
ATOM   4738  CD2 PHE B 294     -10.858  34.005  43.757  1.00 22.42           C  
ANISOU 4738  CD2 PHE B 294     2920   2673   2923   -164   -108   -121       C  
ATOM   4739  CE1 PHE B 294      -9.852  36.162  42.330  1.00 27.70           C  
ANISOU 4739  CE1 PHE B 294     3578   3316   3631   -160   -106   -113       C  
ATOM   4740  CE2 PHE B 294     -10.232  33.799  42.506  1.00 21.67           C  
ANISOU 4740  CE2 PHE B 294     2820   2580   2835   -168   -115   -111       C  
ATOM   4741  CZ  PHE B 294      -9.723  34.877  41.811  1.00 30.83           C  
ANISOU 4741  CZ  PHE B 294     3975   3728   4012   -165   -114   -106       C  
ATOM   4742  N   ALA B 295     -14.755  34.752  45.032  1.00 17.20           N  
ANISOU 4742  N   ALA B 295     2245   2023   2269   -146    -71   -120       N  
ATOM   4743  CA  ALA B 295     -15.730  34.096  44.161  1.00 17.21           C  
ANISOU 4743  CA  ALA B 295     2226   2038   2273   -149    -70   -111       C  
ATOM   4744  C   ALA B 295     -16.784  35.058  43.625  1.00 17.34           C  
ANISOU 4744  C   ALA B 295     2225   2060   2304   -136    -65   -103       C  
ATOM   4745  O   ALA B 295     -17.393  34.775  42.588  1.00 20.91           O  
ANISOU 4745  O   ALA B 295     2657   2530   2759   -135    -71    -96       O  
ATOM   4746  CB  ALA B 295     -16.427  32.951  44.902  1.00 22.17           C  
ANISOU 4746  CB  ALA B 295     2855   2672   2896   -156    -56   -113       C  
ATOM   4747  N   LYS B 296     -17.037  36.163  44.316  1.00 19.56           N  
ANISOU 4747  N   LYS B 296     2511   2328   2594   -124    -53   -106       N  
ATOM   4748  CA  LYS B 296     -18.044  37.103  43.849  1.00 18.75           C  
ANISOU 4748  CA  LYS B 296     2390   2228   2505   -106    -45    -95       C  
ATOM   4749  C   LYS B 296     -17.626  37.798  42.555  1.00 21.43           C  
ANISOU 4749  C   LYS B 296     2722   2567   2852    -96    -53    -78       C  
ATOM   4750  O   LYS B 296     -18.460  38.477  41.945  1.00 19.96           O  
ANISOU 4750  O   LYS B 296     2519   2389   2676    -77    -48    -63       O  
ATOM   4751  CB  LYS B 296     -18.330  38.117  44.961  1.00 19.18           C  
ANISOU 4751  CB  LYS B 296     2455   2263   2569    -96    -26   -105       C  
ATOM   4752  CG  LYS B 296     -18.944  37.407  46.179  1.00 18.05           C  
ANISOU 4752  CG  LYS B 296     2317   2126   2414   -101    -13   -116       C  
ATOM   4753  CD  LYS B 296     -19.248  38.418  47.355  1.00 19.09           C  
ANISOU 4753  CD  LYS B 296     2461   2242   2550    -88      8   -130       C  
ATOM   4754  CE  LYS B 296     -19.415  37.694  48.734  1.00 18.54           C  
ANISOU 4754  CE  LYS B 296     2407   2178   2459    -92     20   -143       C  
ATOM   4755  NZ  LYS B 296     -20.478  36.696  48.754  1.00 18.15           N  
ANISOU 4755  NZ  LYS B 296     2343   2144   2410    -95     31   -132       N  
ATOM   4756  N   THR B 297     -16.366  37.651  42.130  1.00 20.09           N  
ANISOU 4756  N   THR B 297     2565   2390   2679   -105    -64    -78       N  
ATOM   4757  CA  THR B 297     -16.001  38.134  40.800  1.00 19.26           C  
ANISOU 4757  CA  THR B 297     2453   2288   2578    -94    -68    -58       C  
ATOM   4758  C   THR B 297     -16.760  37.415  39.698  1.00 19.67           C  
ANISOU 4758  C   THR B 297     2484   2376   2615    -89    -82    -48       C  
ATOM   4759  O   THR B 297     -16.768  37.890  38.554  1.00 22.58           O  
ANISOU 4759  O   THR B 297     2842   2756   2980    -72    -85    -28       O  
ATOM   4760  CB  THR B 297     -14.490  37.984  40.525  1.00 21.68           C  
ANISOU 4760  CB  THR B 297     2774   2581   2883   -106    -75    -61       C  
ATOM   4761  OG1 THR B 297     -14.101  36.616  40.675  1.00 23.00           O  
ANISOU 4761  OG1 THR B 297     2945   2761   3032   -124    -89    -73       O  
ATOM   4762  CG2 THR B 297     -13.680  38.870  41.455  1.00 21.67           C  
ANISOU 4762  CG2 THR B 297     2787   2547   2900   -110    -64    -75       C  
ATOM   4763  N   SER B 298     -17.383  36.278  40.023  1.00 19.80           N  
ANISOU 4763  N   SER B 298     2492   2409   2622   -104    -88    -63       N  
ATOM   4764  CA  SER B 298     -18.206  35.526  39.098  1.00 22.32           C  
ANISOU 4764  CA  SER B 298     2786   2763   2930   -105   -100    -64       C  
ATOM   4765  C   SER B 298     -19.296  36.363  38.457  1.00 19.48           C  
ANISOU 4765  C   SER B 298     2402   2427   2574    -78   -101    -48       C  
ATOM   4766  O   SER B 298     -19.762  36.013  37.368  1.00 21.01           O  
ANISOU 4766  O   SER B 298     2573   2656   2753    -71   -117    -45       O  
ATOM   4767  CB  SER B 298     -18.861  34.358  39.840  1.00 21.26           C  
ANISOU 4767  CB  SER B 298     2645   2634   2798   -126    -97    -85       C  
ATOM   4768  OG  SER B 298     -19.597  34.850  40.956  1.00 20.12           O  
ANISOU 4768  OG  SER B 298     2500   2477   2666   -120    -79    -86       O  
ATOM   4769  N   ALA B 299     -19.733  37.438  39.111  1.00 19.70           N  
ANISOU 4769  N   ALA B 299     2431   2437   2618    -61    -84    -38       N  
ATOM   4770  CA  ALA B 299     -20.787  38.262  38.513  1.00 21.36           C  
ANISOU 4770  CA  ALA B 299     2615   2667   2832    -31    -82    -18       C  
ATOM   4771  C   ALA B 299     -20.277  39.130  37.371  1.00 24.99           C  
ANISOU 4771  C   ALA B 299     3078   3132   3286     -4    -83     12       C  
ATOM   4772  O   ALA B 299     -21.090  39.724  36.656  1.00 25.55           O  
ANISOU 4772  O   ALA B 299     3126   3228   3353     28    -84     35       O  
ATOM   4773  CB  ALA B 299     -21.438  39.164  39.571  1.00 21.82           C  
ANISOU 4773  CB  ALA B 299     2675   2702   2912    -18    -58    -15       C  
ATOM   4774  N   VAL B 300     -18.960  39.242  37.199  1.00 20.03           N  
ANISOU 4774  N   VAL B 300     2474   2478   2657    -12    -80     16       N  
ATOM   4775  CA  VAL B 300     -18.373  40.224  36.297  1.00 21.95           C  
ANISOU 4775  CA  VAL B 300     2725   2713   2903     14    -71     47       C  
ATOM   4776  C   VAL B 300     -17.617  39.580  35.141  1.00 23.64           C  
ANISOU 4776  C   VAL B 300     2941   2950   3090     11    -87     53       C  
ATOM   4777  O   VAL B 300     -17.619  40.113  34.027  1.00 25.36           O  
ANISOU 4777  O   VAL B 300     3153   3187   3296     41    -85     83       O  
ATOM   4778  CB  VAL B 300     -17.449  41.202  37.073  1.00 31.46           C  
ANISOU 4778  CB  VAL B 300     3955   3862   4138      9    -45     48       C  
ATOM   4779  CG1 VAL B 300     -16.811  42.215  36.128  1.00 47.10           C  
ANISOU 4779  CG1 VAL B 300     5942   5826   6128     34    -27     83       C  
ATOM   4780  CG2 VAL B 300     -18.228  41.907  38.189  1.00 34.44           C  
ANISOU 4780  CG2 VAL B 300     4330   4217   4539     15    -26     40       C  
ATOM   4781  N   TYR B 301     -16.913  38.466  35.382  1.00 22.70           N  
ANISOU 4781  N   TYR B 301     2833   2830   2963    -22    -99     26       N  
ATOM   4782  CA  TYR B 301     -15.820  38.145  34.461  1.00 25.01           C  
ANISOU 4782  CA  TYR B 301     3136   3126   3241    -24   -104     33       C  
ATOM   4783  C   TYR B 301     -16.291  37.561  33.125  1.00 22.49           C  
ANISOU 4783  C   TYR B 301     2798   2859   2886    -10   -124     38       C  
ATOM   4784  O   TYR B 301     -15.563  37.670  32.129  1.00 22.58           O  
ANISOU 4784  O   TYR B 301     2817   2880   2882      2   -123     56       O  
ATOM   4785  CB  TYR B 301     -14.798  37.213  35.139  1.00 20.10           C  
ANISOU 4785  CB  TYR B 301     2532   2483   2623    -59   -109      6       C  
ATOM   4786  CG  TYR B 301     -15.248  35.777  35.314  1.00 23.70           C  
ANISOU 4786  CG  TYR B 301     2979   2962   3064    -82   -126    -22       C  
ATOM   4787  CD1 TYR B 301     -15.250  34.885  34.239  1.00 22.19           C  
ANISOU 4787  CD1 TYR B 301     2779   2804   2849    -85   -141    -30       C  
ATOM   4788  CD2 TYR B 301     -15.604  35.296  36.562  1.00 24.59           C  
ANISOU 4788  CD2 TYR B 301     3094   3060   3189   -102   -123    -43       C  
ATOM   4789  CE1 TYR B 301     -15.674  33.582  34.395  1.00 22.76           C  
ANISOU 4789  CE1 TYR B 301     2842   2891   2915   -109   -152    -59       C  
ATOM   4790  CE2 TYR B 301     -16.011  33.985  36.735  1.00 23.98           C  
ANISOU 4790  CE2 TYR B 301     3009   2996   3104   -123   -131    -66       C  
ATOM   4791  CZ  TYR B 301     -16.055  33.138  35.649  1.00 25.27           C  
ANISOU 4791  CZ  TYR B 301     3162   3189   3251   -128   -145    -75       C  
ATOM   4792  OH  TYR B 301     -16.476  31.850  35.821  1.00 27.98           O  
ANISOU 4792  OH  TYR B 301     3496   3540   3595   -151   -148   -102       O  
ATOM   4793  N   ASN B 302     -17.459  36.911  33.063  1.00 20.58           N  
ANISOU 4793  N   ASN B 302     2532   2655   2632    -13   -142     20       N  
ATOM   4794  CA  ASN B 302     -17.829  36.257  31.804  1.00 21.77           C  
ANISOU 4794  CA  ASN B 302     2663   2861   2748     -4   -164     14       C  
ATOM   4795  C   ASN B 302     -18.040  37.250  30.664  1.00 20.89           C  
ANISOU 4795  C   ASN B 302     2544   2780   2615     43   -163     54       C  
ATOM   4796  O   ASN B 302     -17.540  36.991  29.554  1.00 22.26           O  
ANISOU 4796  O   ASN B 302     2720   2981   2757     55   -171     61       O  
ATOM   4797  CB  ASN B 302     -19.042  35.346  32.003  1.00 24.09           C  
ANISOU 4797  CB  ASN B 302     2927   3188   3039    -20   -183    -20       C  
ATOM   4798  CG  ASN B 302     -18.656  34.016  32.595  1.00 26.33           C  
ANISOU 4798  CG  ASN B 302     3219   3453   3331    -63   -185    -57       C  
ATOM   4799  OD1 ASN B 302     -17.905  33.245  31.984  1.00 25.44           O  
ANISOU 4799  OD1 ASN B 302     3116   3347   3204    -76   -192    -71       O  
ATOM   4800  ND2 ASN B 302     -19.123  33.750  33.808  1.00 25.97           N  
ANISOU 4800  ND2 ASN B 302     3172   3383   3312    -83   -174    -72       N  
ATOM   4801  N   PRO B 303     -18.759  38.367  30.832  1.00 21.19           N  
ANISOU 4801  N   PRO B 303     2571   2815   2664     75   -151     83       N  
ATOM   4802  CA  PRO B 303     -18.832  39.334  29.721  1.00 23.20           C  
ANISOU 4802  CA  PRO B 303     2822   3095   2898    125   -144    130       C  
ATOM   4803  C   PRO B 303     -17.470  39.880  29.323  1.00 26.50           C  
ANISOU 4803  C   PRO B 303     3271   3476   3321    132   -120    158       C  
ATOM   4804  O   PRO B 303     -17.286  40.254  28.158  1.00 26.09           O  
ANISOU 4804  O   PRO B 303     3220   3454   3239    168   -116    192       O  
ATOM   4805  CB  PRO B 303     -19.759  40.444  30.256  1.00 25.82           C  
ANISOU 4805  CB  PRO B 303     3141   3413   3254    154   -127    155       C  
ATOM   4806  CG  PRO B 303     -20.481  39.844  31.407  1.00 32.78           C  
ANISOU 4806  CG  PRO B 303     4010   4287   4158    120   -136    116       C  
ATOM   4807  CD  PRO B 303     -19.602  38.776  31.982  1.00 24.22           C  
ANISOU 4807  CD  PRO B 303     2946   3177   3080     71   -141     78       C  
ATOM   4808  N   VAL B 304     -16.507  39.938  30.252  1.00 24.85           N  
ANISOU 4808  N   VAL B 304     3086   3208   3147    100   -101    146       N  
ATOM   4809  CA  VAL B 304     -15.169  40.423  29.898  1.00 27.75           C  
ANISOU 4809  CA  VAL B 304     3478   3539   3525    103    -77    168       C  
ATOM   4810  C   VAL B 304     -14.475  39.444  28.960  1.00 24.18           C  
ANISOU 4810  C   VAL B 304     3032   3118   3038     94    -92    158       C  
ATOM   4811  O   VAL B 304     -13.869  39.846  27.960  1.00 21.59           O  
ANISOU 4811  O   VAL B 304     2712   2797   2694    120    -78    190       O  
ATOM   4812  CB  VAL B 304     -14.315  40.681  31.156  1.00 27.30           C  
ANISOU 4812  CB  VAL B 304     3442   3418   3515     69    -58    150       C  
ATOM   4813  CG1 VAL B 304     -12.851  41.133  30.733  1.00 30.94           C  
ANISOU 4813  CG1 VAL B 304     3922   3842   3992     68    -33    170       C  
ATOM   4814  CG2 VAL B 304     -14.981  41.699  32.054  1.00 22.16           C  
ANISOU 4814  CG2 VAL B 304     2787   2735   2898     79    -40    157       C  
ATOM   4815  N   ILE B 305     -14.568  38.142  29.248  1.00 22.70           N  
ANISOU 4815  N   ILE B 305     2838   2948   2838     60   -118    114       N  
ATOM   4816  CA  ILE B 305     -14.064  37.144  28.308  1.00 23.45           C  
ANISOU 4816  CA  ILE B 305     2936   3076   2898     53   -134     98       C  
ATOM   4817  C   ILE B 305     -14.741  37.298  26.950  1.00 24.52           C  
ANISOU 4817  C   ILE B 305     3054   3275   2986     94   -146    119       C  
ATOM   4818  O   ILE B 305     -14.102  37.214  25.895  1.00 25.11           O  
ANISOU 4818  O   ILE B 305     3138   3371   3030    111   -142    134       O  
ATOM   4819  CB  ILE B 305     -14.269  35.724  28.879  1.00 22.98           C  
ANISOU 4819  CB  ILE B 305     2870   3023   2839     11   -156     47       C  
ATOM   4820  CG1 ILE B 305     -13.503  35.536  30.195  1.00 25.27           C  
ANISOU 4820  CG1 ILE B 305     3178   3256   3169    -24   -143     31       C  
ATOM   4821  CG2 ILE B 305     -13.879  34.671  27.817  1.00 23.87           C  
ANISOU 4821  CG2 ILE B 305     2981   3172   2914      5   -170     26       C  
ATOM   4822  CD1 ILE B 305     -13.801  34.166  30.907  1.00 25.00           C  
ANISOU 4822  CD1 ILE B 305     3137   3222   3138    -61   -158    -13       C  
ATOM   4823  N   TYR B 306     -16.060  37.480  26.965  1.00 22.31           N  
ANISOU 4823  N   TYR B 306     2749   3032   2697    111   -163    117       N  
ATOM   4824  CA  TYR B 306     -16.869  37.535  25.746  1.00 23.22           C  
ANISOU 4824  CA  TYR B 306     2841   3221   2762    152   -183    130       C  
ATOM   4825  C   TYR B 306     -16.405  38.648  24.814  1.00 23.13           C  
ANISOU 4825  C   TYR B 306     2843   3214   2732    203   -158    190       C  
ATOM   4826  O   TYR B 306     -16.270  38.455  23.594  1.00 25.89           O  
ANISOU 4826  O   TYR B 306     3191   3615   3031    231   -167    202       O  
ATOM   4827  CB  TYR B 306     -18.315  37.764  26.184  1.00 21.88           C  
ANISOU 4827  CB  TYR B 306     2639   3077   2599    162   -199    123       C  
ATOM   4828  CG  TYR B 306     -19.426  37.549  25.178  1.00 24.21           C  
ANISOU 4828  CG  TYR B 306     2897   3457   2844    194   -231    117       C  
ATOM   4829  CD1 TYR B 306     -19.262  36.764  24.037  1.00 21.99           C  
ANISOU 4829  CD1 TYR B 306     2609   3234   2512    199   -255     96       C  
ATOM   4830  CD2 TYR B 306     -20.679  38.098  25.434  1.00 22.54           C  
ANISOU 4830  CD2 TYR B 306     2655   3270   2640    218   -239    128       C  
ATOM   4831  CE1 TYR B 306     -20.336  36.563  23.151  1.00 23.67           C  
ANISOU 4831  CE1 TYR B 306     2783   3533   2678    228   -290     83       C  
ATOM   4832  CE2 TYR B 306     -21.734  37.903  24.579  1.00 25.77           C  
ANISOU 4832  CE2 TYR B 306     3024   3762   3006    248   -272    119       C  
ATOM   4833  CZ  TYR B 306     -21.565  37.139  23.449  1.00 26.79           C  
ANISOU 4833  CZ  TYR B 306     3145   3952   3081    252   -299     95       C  
ATOM   4834  OH  TYR B 306     -22.670  36.981  22.638  1.00 30.32           O  
ANISOU 4834  OH  TYR B 306     3548   4488   3485    282   -336     82       O  
ATOM   4835  N   ILE B 307     -16.190  39.831  25.382  1.00 23.30           N  
ANISOU 4835  N   ILE B 307     2877   3182   2793    218   -124    230       N  
ATOM   4836  CA  ILE B 307     -15.715  40.977  24.617  1.00 25.76           C  
ANISOU 4836  CA  ILE B 307     3204   3484   3101    266    -90    292       C  
ATOM   4837  C   ILE B 307     -14.322  40.704  24.077  1.00 20.81           C  
ANISOU 4837  C   ILE B 307     2602   2836   2467    255    -72    298       C  
ATOM   4838  O   ILE B 307     -14.002  41.071  22.951  1.00 26.74           O  
ANISOU 4838  O   ILE B 307     3361   3614   3184    296    -58    338       O  
ATOM   4839  CB  ILE B 307     -15.732  42.230  25.508  1.00 24.79           C  
ANISOU 4839  CB  ILE B 307     3090   3295   3036    273    -53    322       C  
ATOM   4840  CG1 ILE B 307     -17.165  42.643  25.820  1.00 27.40           C  
ANISOU 4840  CG1 ILE B 307     3394   3651   3366    298    -65    328       C  
ATOM   4841  CG2 ILE B 307     -14.997  43.368  24.835  1.00 35.89           C  
ANISOU 4841  CG2 ILE B 307     4515   4670   4451    313     -7    384       C  
ATOM   4842  CD1 ILE B 307     -17.255  43.677  26.958  1.00 36.04           C  
ANISOU 4842  CD1 ILE B 307     4495   4675   4522    293    -32    341       C  
ATOM   4843  N  AMET B 308     -13.474  40.053  24.876  0.49 25.78           N  
ANISOU 4843  N  AMET B 308     3246   3421   3129    202    -72    259       N  
ATOM   4844  N  BMET B 308     -13.475  40.055  24.870  0.51 25.77           N  
ANISOU 4844  N  BMET B 308     3244   3420   3127    202    -72    260       N  
ATOM   4845  CA AMET B 308     -12.094  39.817  24.453  0.49 30.14           C  
ANISOU 4845  CA AMET B 308     3820   3950   3682    190    -53    264       C  
ATOM   4846  CA BMET B 308     -12.101  39.825  24.434  0.51 30.13           C  
ANISOU 4846  CA BMET B 308     3819   3950   3681    191    -52    265       C  
ATOM   4847  C  AMET B 308     -11.977  38.710  23.410  0.49 32.99           C  
ANISOU 4847  C  AMET B 308     4179   4371   3986    192    -78    242       C  
ATOM   4848  C  BMET B 308     -11.967  38.696  23.422  0.51 33.02           C  
ANISOU 4848  C  BMET B 308     4182   4374   3991    191    -78    242       C  
ATOM   4849  O  AMET B 308     -11.044  38.728  22.601  0.49 31.52           O  
ANISOU 4849  O  AMET B 308     4008   4184   3783    205    -58    263       O  
ATOM   4850  O  BMET B 308     -11.005  38.689  22.647  0.51 31.54           O  
ANISOU 4850  O  BMET B 308     4010   4184   3787    202    -58    261       O  
ATOM   4851  CB AMET B 308     -11.218  39.466  25.664  0.49 31.31           C  
ANISOU 4851  CB AMET B 308     3979   4035   3881    137    -46    230       C  
ATOM   4852  CB BMET B 308     -11.211  39.527  25.642  0.51 31.30           C  
ANISOU 4852  CB BMET B 308     3979   4033   3881    139    -45    232       C  
ATOM   4853  CG AMET B 308     -10.951  40.620  26.627  0.49 37.85           C  
ANISOU 4853  CG AMET B 308     4815   4797   4769    132    -15    248       C  
ATOM   4854  CG BMET B 308     -11.035  40.720  26.546  0.51 37.78           C  
ANISOU 4854  CG BMET B 308     4806   4791   4758    138    -14    253       C  
ATOM   4855  SD AMET B 308      -9.993  40.115  28.087  0.49 41.50           S  
ANISOU 4855  SD AMET B 308     5286   5201   5280     73    -17    200       S  
ATOM   4856  SD BMET B 308     -10.254  42.070  25.655  0.51 51.66           S  
ANISOU 4856  SD BMET B 308     6578   6520   6532    180     40    319       S  
ATOM   4857  CE AMET B 308      -8.800  39.017  27.343  0.49 40.81           C  
ANISOU 4857  CE AMET B 308     5208   5128   5168     56    -22    187       C  
ATOM   4858  CE BMET B 308      -8.727  41.294  25.141  0.51 35.74           C  
ANISOU 4858  CE BMET B 308     4575   4494   4509    156     47    307       C  
ATOM   4859  N   MET B 309     -12.897  37.745  23.402  1.00 23.48           N  
ANISOU 4859  N   MET B 309     2953   3215   2752    178   -118    198       N  
ATOM   4860  CA  MET B 309     -12.715  36.539  22.619  1.00 25.41           C  
ANISOU 4860  CA  MET B 309     3195   3505   2953    167   -141    162       C  
ATOM   4861  C   MET B 309     -13.784  36.272  21.572  1.00 36.73           C  
ANISOU 4861  C   MET B 309     4605   5027   4325    200   -172    154       C  
ATOM   4862  O   MET B 309     -13.724  35.226  20.914  1.00 34.32           O  
ANISOU 4862  O   MET B 309     4295   4763   3982    189   -194    114       O  
ATOM   4863  CB  MET B 309     -12.602  35.327  23.553  1.00 28.56           C  
ANISOU 4863  CB  MET B 309     3593   3880   3380    109   -158    102       C  
ATOM   4864  CG  MET B 309     -11.469  35.478  24.565  1.00 28.12           C  
ANISOU 4864  CG  MET B 309     3558   3748   3378     78   -132    106       C  
ATOM   4865  SD  MET B 309     -11.058  33.936  25.367  1.00 27.02           S  
ANISOU 4865  SD  MET B 309     3422   3586   3257     21   -147     46       S  
ATOM   4866  CE  MET B 309     -10.347  32.998  23.993  1.00 25.71           C  
ANISOU 4866  CE  MET B 309     3264   3458   3045     27   -150     30       C  
ATOM   4867  N   ASN B 310     -14.767  37.150  21.398  1.00 23.92           N  
ANISOU 4867  N   ASN B 310     2964   3434   2689    242   -177    186       N  
ATOM   4868  CA  ASN B 310     -15.726  36.968  20.319  1.00 23.86           C  
ANISOU 4868  CA  ASN B 310     2932   3518   2617    280   -208    182       C  
ATOM   4869  C   ASN B 310     -15.766  38.249  19.493  1.00 31.19           C  
ANISOU 4869  C   ASN B 310     3866   4468   3517    350   -185    257       C  
ATOM   4870  O   ASN B 310     -16.250  39.293  19.954  1.00 26.33           O  
ANISOU 4870  O   ASN B 310     3246   3829   2930    375   -167    298       O  
ATOM   4871  CB  ASN B 310     -17.111  36.598  20.836  1.00 24.49           C  
ANISOU 4871  CB  ASN B 310     2972   3630   2701    266   -244    143       C  
ATOM   4872  CG  ASN B 310     -18.022  36.158  19.730  1.00 29.20           C  
ANISOU 4872  CG  ASN B 310     3537   4327   3231    296   -284    120       C  
ATOM   4873  OD1 ASN B 310     -18.743  36.965  19.142  1.00 29.47           O  
ANISOU 4873  OD1 ASN B 310     3553   4413   3231    353   -291    160       O  
ATOM   4874  ND2 ASN B 310     -17.958  34.868  19.392  1.00 31.50           N  
ANISOU 4874  ND2 ASN B 310     3820   4650   3500    261   -311     55       N  
ATOM   4875  N   LYS B 311     -15.238  38.164  18.278  1.00 31.40           N  
ANISOU 4875  N   LYS B 311     3904   4538   3487    384   -180    276       N  
ATOM   4876  CA  LYS B 311     -15.087  39.357  17.460  1.00 29.69           C  
ANISOU 4876  CA  LYS B 311     3701   4336   3245    452   -147    355       C  
ATOM   4877  C   LYS B 311     -16.441  39.893  17.026  1.00 31.56           C  
ANISOU 4877  C   LYS B 311     3905   4645   3441    507   -171    379       C  
ATOM   4878  O   LYS B 311     -16.647  41.110  16.975  1.00 34.43           O  
ANISOU 4878  O   LYS B 311     4272   4992   3816    557   -140    447       O  
ATOM   4879  CB  LYS B 311     -14.181  39.033  16.276  1.00 32.11           C  
ANISOU 4879  CB  LYS B 311     4029   4675   3498    474   -135    367       C  
ATOM   4880  CG  LYS B 311     -14.149  40.066  15.159  1.00 42.75           C  
ANISOU 4880  CG  LYS B 311     5386   6061   4795    554   -106    447       C  
ATOM   4881  CD  LYS B 311     -13.314  39.533  13.982  1.00 48.24           C  
ANISOU 4881  CD  LYS B 311     6102   6799   5430    572    -98    447       C  
ATOM   4882  CE  LYS B 311     -13.305  40.501  12.799  1.00 63.73           C  
ANISOU 4882  CE  LYS B 311     8075   8808   7333    659    -68    530       C  
ATOM   4883  NZ  LYS B 311     -12.631  39.903  11.600  1.00 79.14           N  
ANISOU 4883  NZ  LYS B 311    10043  10814   9213    680    -65    525       N  
ATOM   4884  N   GLN B 312     -17.390  39.005  16.724  1.00 30.60           N  
ANISOU 4884  N   GLN B 312     3749   4601   3275    500   -226    323       N  
ATOM   4885  CA  GLN B 312     -18.705  39.473  16.298  1.00 28.04           C  
ANISOU 4885  CA  GLN B 312     3388   4355   2912    554   -254    342       C  
ATOM   4886  C   GLN B 312     -19.412  40.240  17.409  1.00 32.58           C  
ANISOU 4886  C   GLN B 312     3949   4879   3550    550   -242    362       C  
ATOM   4887  O   GLN B 312     -19.982  41.312  17.177  1.00 31.82           O  
ANISOU 4887  O   GLN B 312     3844   4799   3446    610   -228    423       O  
ATOM   4888  CB  GLN B 312     -19.546  38.291  15.830  1.00 32.76           C  
ANISOU 4888  CB  GLN B 312     3947   5043   3459    537   -315    265       C  
ATOM   4889  CG  GLN B 312     -20.962  38.659  15.490  1.00 33.68           C  
ANISOU 4889  CG  GLN B 312     4016   5244   3538    585   -351    273       C  
ATOM   4890  CD  GLN B 312     -21.758  37.459  15.021  1.00 49.81           C  
ANISOU 4890  CD  GLN B 312     6016   7376   5535    562   -412    188       C  
ATOM   4891  OE1 GLN B 312     -22.056  36.553  15.802  1.00 50.99           O  
ANISOU 4891  OE1 GLN B 312     6146   7499   5727    495   -432    117       O  
ATOM   4892  NE2 GLN B 312     -22.097  37.440  13.735  1.00 49.23           N  
ANISOU 4892  NE2 GLN B 312     5924   7409   5373    619   -441    193       N  
ATOM   4893  N   PHE B 313     -19.397  39.701  18.624  1.00 29.57           N  
ANISOU 4893  N   PHE B 313     3566   4436   3232    482   -246    311       N  
ATOM   4894  CA  PHE B 313     -20.034  40.404  19.733  1.00 30.92           C  
ANISOU 4894  CA  PHE B 313     3727   4558   3463    476   -232    326       C  
ATOM   4895  C   PHE B 313     -19.348  41.739  20.023  1.00 30.62           C  
ANISOU 4895  C   PHE B 313     3722   4444   3467    504   -174    399       C  
ATOM   4896  O   PHE B 313     -20.017  42.774  20.191  1.00 28.11           O  
ANISOU 4896  O   PHE B 313     3394   4120   3165    547   -157    446       O  
ATOM   4897  CB  PHE B 313     -20.040  39.537  20.986  1.00 28.56           C  
ANISOU 4897  CB  PHE B 313     3425   4207   3219    399   -243    260       C  
ATOM   4898  CG  PHE B 313     -20.668  40.228  22.154  1.00 29.13           C  
ANISOU 4898  CG  PHE B 313     3488   4230   3349    392   -228    273       C  
ATOM   4899  CD1 PHE B 313     -22.043  40.399  22.207  1.00 33.21           C  
ANISOU 4899  CD1 PHE B 313     3963   4798   3858    416   -252    269       C  
ATOM   4900  CD2 PHE B 313     -19.886  40.777  23.152  1.00 23.02           C  
ANISOU 4900  CD2 PHE B 313     2746   3362   2637    367   -187    289       C  
ATOM   4901  CE1 PHE B 313     -22.641  41.065  23.270  1.00 34.21           C  
ANISOU 4901  CE1 PHE B 313     4082   4879   4038    414   -234    281       C  
ATOM   4902  CE2 PHE B 313     -20.480  41.452  24.213  1.00 29.48           C  
ANISOU 4902  CE2 PHE B 313     3558   4137   3506    364   -171    298       C  
ATOM   4903  CZ  PHE B 313     -21.851  41.600  24.265  1.00 29.70           C  
ANISOU 4903  CZ  PHE B 313     3547   4213   3525    388   -193    296       C  
ATOM   4904  N   ARG B 314     -18.011  41.738  20.059  1.00 27.23           N  
ANISOU 4904  N   ARG B 314     3331   3956   3060    480   -140    408       N  
ATOM   4905  CA  ARG B 314     -17.272  42.970  20.336  1.00 30.12           C  
ANISOU 4905  CA  ARG B 314     3727   4244   3474    500    -82    470       C  
ATOM   4906  C   ARG B 314     -17.596  44.045  19.299  1.00 32.73           C  
ANISOU 4906  C   ARG B 314     4057   4613   3767    584    -57    550       C  
ATOM   4907  O   ARG B 314     -17.801  45.220  19.650  1.00 31.60           O  
ANISOU 4907  O   ARG B 314     3919   4424   3665    615    -18    602       O  
ATOM   4908  CB  ARG B 314     -15.767  42.652  20.391  1.00 31.29           C  
ANISOU 4908  CB  ARG B 314     3909   4335   3644    461    -55    460       C  
ATOM   4909  CG  ARG B 314     -14.829  43.841  20.291  1.00 42.94           C  
ANISOU 4909  CG  ARG B 314     5414   5743   5158    486      8    525       C  
ATOM   4910  CD  ARG B 314     -13.365  43.446  20.585  1.00 30.94           C  
ANISOU 4910  CD  ARG B 314     3920   4162   3672    436     31    504       C  
ATOM   4911  NE  ARG B 314     -12.695  42.792  19.472  1.00 36.86           N  
ANISOU 4911  NE  ARG B 314     4681   4956   4368    447     26    504       N  
ATOM   4912  CZ  ARG B 314     -12.401  41.501  19.427  1.00 34.98           C  
ANISOU 4912  CZ  ARG B 314     4441   4744   4105    406     -8    445       C  
ATOM   4913  NH1 ARG B 314     -12.696  40.687  20.430  1.00 36.90           N  
ANISOU 4913  NH1 ARG B 314     4673   4974   4375    350    -41    382       N  
ATOM   4914  NH2 ARG B 314     -11.785  41.014  18.356  1.00 38.03           N  
ANISOU 4914  NH2 ARG B 314     4839   5170   4441    422     -6    450       N  
ATOM   4915  N   ASN B 315     -17.711  43.655  18.025  1.00 32.31           N  
ANISOU 4915  N   ASN B 315     3997   4645   3634    625    -80    560       N  
ATOM   4916  CA  ASN B 315     -18.047  44.631  16.991  1.00 34.45           C  
ANISOU 4916  CA  ASN B 315     4267   4962   3860    712    -58    640       C  
ATOM   4917  C   ASN B 315     -19.471  45.141  17.126  1.00 37.94           C  
ANISOU 4917  C   ASN B 315     4673   5449   4294    755    -79    657       C  
ATOM   4918  O   ASN B 315     -19.724  46.333  16.908  1.00 37.85           O  
ANISOU 4918  O   ASN B 315     4665   5424   4292    818    -40    733       O  
ATOM   4919  CB  ASN B 315     -17.828  44.038  15.599  1.00 37.48           C  
ANISOU 4919  CB  ASN B 315     4652   5436   4152    748    -80    642       C  
ATOM   4920  CG  ASN B 315     -16.367  43.814  15.301  1.00 42.09           C  
ANISOU 4920  CG  ASN B 315     5275   5973   4743    724    -44    647       C  
ATOM   4921  OD1 ASN B 315     -15.490  44.242  16.061  1.00 48.55           O  
ANISOU 4921  OD1 ASN B 315     6118   6692   5636    688      1    658       O  
ATOM   4922  ND2 ASN B 315     -16.091  43.136  14.201  1.00 49.57           N  
ANISOU 4922  ND2 ASN B 315     6226   6994   5615    743    -64    635       N  
ATOM   4923  N   CYS B 316     -20.426  44.258  17.454  1.00 34.41           N  
ANISOU 4923  N   CYS B 316     4187   5055   3831    725   -138    590       N  
ATOM   4924  CA  CYS B 316     -21.787  44.721  17.708  1.00 36.27           C  
ANISOU 4924  CA  CYS B 316     4384   5329   4069    759   -158    602       C  
ATOM   4925  C   CYS B 316     -21.829  45.688  18.877  1.00 35.87           C  
ANISOU 4925  C   CYS B 316     4345   5179   4105    748   -112    630       C  
ATOM   4926  O   CYS B 316     -22.603  46.651  18.865  1.00 35.25           O  
ANISOU 4926  O   CYS B 316     4251   5108   4034    805    -96    682       O  
ATOM   4927  CB  CYS B 316     -22.728  43.549  17.988  1.00 34.86           C  
ANISOU 4927  CB  CYS B 316     4161   5211   3873    716   -223    517       C  
ATOM   4928  SG  CYS B 316     -23.039  42.459  16.598  1.00 43.87           S  
ANISOU 4928  SG  CYS B 316     5274   6485   4910    735   -285    474       S  
ATOM   4929  N   MET B 317     -21.050  45.414  19.922  1.00 32.01           N  
ANISOU 4929  N   MET B 317     3880   4601   3680    677    -94    591       N  
ATOM   4930  CA  MET B 317     -21.051  46.293  21.079  1.00 37.56           C  
ANISOU 4930  CA  MET B 317     4596   5213   4464    662    -52    607       C  
ATOM   4931  C   MET B 317     -20.506  47.671  20.718  1.00 37.24           C  
ANISOU 4931  C   MET B 317     4583   5120   4448    716     14    692       C  
ATOM   4932  O   MET B 317     -21.058  48.691  21.145  1.00 37.85           O  
ANISOU 4932  O   MET B 317     4656   5162   4565    749     46    732       O  
ATOM   4933  CB  MET B 317     -20.246  45.674  22.223  1.00 28.65           C  
ANISOU 4933  CB  MET B 317     3488   4008   3391    577    -48    546       C  
ATOM   4934  CG  MET B 317     -20.328  46.489  23.511  1.00 42.41           C  
ANISOU 4934  CG  MET B 317     5239   5663   5212    557    -12    550       C  
ATOM   4935  SD  MET B 317     -19.354  45.736  24.815  1.00 54.24           S  
ANISOU 4935  SD  MET B 317     6760   7085   6762    464    -12    479       S  
ATOM   4936  CE  MET B 317     -17.753  45.799  24.031  1.00 56.75           C  
ANISOU 4936  CE  MET B 317     7115   7374   7074    462     19    505       C  
ATOM   4937  N   VAL B 318     -19.426  47.723  19.936  1.00 38.64           N  
ANISOU 4937  N   VAL B 318     4790   5287   4604    728     40    722       N  
ATOM   4938  CA  VAL B 318     -18.907  49.011  19.481  1.00 44.25           C  
ANISOU 4938  CA  VAL B 318     5525   5949   5337    783    108    807       C  
ATOM   4939  C   VAL B 318     -19.968  49.748  18.681  1.00 45.79           C  
ANISOU 4939  C   VAL B 318     5699   6210   5488    874    110    875       C  
ATOM   4940  O   VAL B 318     -20.208  50.942  18.893  1.00 48.72           O  
ANISOU 4940  O   VAL B 318     6077   6532   5905    916    161    935       O  
ATOM   4941  CB  VAL B 318     -17.623  48.820  18.660  1.00 42.09           C  
ANISOU 4941  CB  VAL B 318     5283   5667   5041    782    133    826       C  
ATOM   4942  CG1 VAL B 318     -17.257  50.120  17.986  1.00 49.62           C  
ANISOU 4942  CG1 VAL B 318     6259   6587   6008    852    204    923       C  
ATOM   4943  CG2 VAL B 318     -16.517  48.362  19.563  1.00 38.06           C  
ANISOU 4943  CG2 VAL B 318     4794   5077   4590    699    144    771       C  
ATOM   4944  N   THR B 319     -20.635  49.034  17.769  1.00 41.68           N  
ANISOU 4944  N   THR B 319     5152   5805   4880    907     54    864       N  
ATOM   4945  CA  THR B 319     -21.686  49.632  16.944  1.00 42.48           C  
ANISOU 4945  CA  THR B 319     5226   5986   4928    998     47    926       C  
ATOM   4946  C   THR B 319     -22.812  50.201  17.798  1.00 49.37           C  
ANISOU 4946  C   THR B 319     6070   6841   5846   1009     45    928       C  
ATOM   4947  O   THR B 319     -23.300  51.313  17.552  1.00 52.88           O  
ANISOU 4947  O   THR B 319     6511   7280   6299   1082     83   1005       O  
ATOM   4948  CB  THR B 319     -22.226  48.579  15.977  1.00 43.00           C  
ANISOU 4948  CB  THR B 319     5261   6183   4893   1015    -25    889       C  
ATOM   4949  OG1 THR B 319     -21.187  48.212  15.067  1.00 47.39           O  
ANISOU 4949  OG1 THR B 319     5847   6757   5402   1020    -15    899       O  
ATOM   4950  CG2 THR B 319     -23.438  49.091  15.202  1.00 55.85           C  
ANISOU 4950  CG2 THR B 319     6851   7909   6460   1108    -46    942       C  
ATOM   4951  N   THR B 320     -23.255  49.440  18.796  1.00 39.12           N  
ANISOU 4951  N   THR B 320     4751   5535   4578    940      5    848       N  
ATOM   4952  CA  THR B 320     -24.288  49.926  19.707  1.00 42.42           C  
ANISOU 4952  CA  THR B 320     5142   5930   5044    943      6    844       C  
ATOM   4953  C   THR B 320     -23.795  51.119  20.516  1.00 58.10           C  
ANISOU 4953  C   THR B 320     7160   7795   7118    942     81    886       C  
ATOM   4954  O   THR B 320     -24.510  52.113  20.681  1.00 55.81           O  
ANISOU 4954  O   THR B 320     6860   7489   6856    994    112    936       O  
ATOM   4955  CB  THR B 320     -24.720  48.801  20.651  1.00 52.56           C  
ANISOU 4955  CB  THR B 320     6403   7223   6347    863    -46    748       C  
ATOM   4956  OG1 THR B 320     -25.472  47.830  19.920  1.00 50.83           O  
ANISOU 4956  OG1 THR B 320     6141   7119   6053    872   -114    710       O  
ATOM   4957  CG2 THR B 320     -25.550  49.349  21.833  1.00 45.04           C  
ANISOU 4957  CG2 THR B 320     5433   6220   5460    853    -30    740       C  
ATOM   4958  N   LEU B 321     -22.570  51.025  21.044  1.00 43.72           N  
ANISOU 4958  N   LEU B 321     5378   5888   5344    881    112    861       N  
ATOM   4959  CA  LEU B 321     -22.042  52.056  21.929  1.00 52.05           C  
ANISOU 4959  CA  LEU B 321     6462   6825   6489    865    179    881       C  
ATOM   4960  C   LEU B 321     -21.716  53.341  21.175  1.00 57.71           C  
ANISOU 4960  C   LEU B 321     7201   7508   7218    940    249    979       C  
ATOM   4961  O   LEU B 321     -21.720  54.425  21.768  1.00 64.18           O  
ANISOU 4961  O   LEU B 321     8032   8244   8109    952    307   1010       O  
ATOM   4962  CB  LEU B 321     -20.804  51.528  22.651  1.00 54.76           C  
ANISOU 4962  CB  LEU B 321     6835   7097   6874    780    186    823       C  
ATOM   4963  CG  LEU B 321     -20.754  51.561  24.177  1.00 56.06           C  
ANISOU 4963  CG  LEU B 321     7005   7184   7112    713    194    765       C  
ATOM   4964  CD1 LEU B 321     -22.109  51.212  24.746  1.00 55.54           C  
ANISOU 4964  CD1 LEU B 321     6902   7164   7037    713    152    732       C  
ATOM   4965  CD2 LEU B 321     -19.664  50.603  24.699  1.00 49.23           C  
ANISOU 4965  CD2 LEU B 321     6158   6289   6257    632    175    698       C  
ATOM   4966  N   CYS B 322     -21.447  53.247  19.881  1.00 56.53           N  
ANISOU 4966  N   CYS B 322     7056   7422   7001    992    247   1027       N  
ATOM   4967  CA  CYS B 322     -21.059  54.414  19.103  1.00 58.93           C  
ANISOU 4967  CA  CYS B 322     7383   7692   7313   1065    318   1125       C  
ATOM   4968  C   CYS B 322     -22.065  54.707  17.998  1.00 60.66           C  
ANISOU 4968  C   CYS B 322     7577   8014   7456   1167    302   1194       C  
ATOM   4969  O   CYS B 322     -21.680  54.987  16.867  1.00 72.49           O  
ANISOU 4969  O   CYS B 322     9090   9546   8905   1228    327   1261       O  
ATOM   4970  CB  CYS B 322     -19.663  54.202  18.523  1.00 51.62           C  
ANISOU 4970  CB  CYS B 322     6493   6740   6381   1045    346   1134       C  
ATOM   4971  SG  CYS B 322     -18.419  53.864  19.807  1.00 77.31           S  
ANISOU 4971  SG  CYS B 322     9772   9879   9724    929    362   1053       S  
TER    4972      CYS B 322                                                      
HETATM 4973  C1  NAG C   1      10.559  21.857   0.376  1.00 29.78           C  
ANISOU 4973  C1  NAG C   1     4186   4366   2764    456    581    -74       C  
HETATM 4974  C2  NAG C   1       9.084  21.944   0.768  1.00 32.79           C  
ANISOU 4974  C2  NAG C   1     4554   4786   3118    440    508   -109       C  
HETATM 4975  C3  NAG C   1       8.250  20.924  -0.013  1.00 34.66           C  
ANISOU 4975  C3  NAG C   1     4800   5099   3270    443    472   -204       C  
HETATM 4976  C4  NAG C   1       8.520  21.004  -1.507  1.00 33.06           C  
ANISOU 4976  C4  NAG C   1     4625   4975   2960    504    507   -198       C  
HETATM 4977  C5  NAG C   1      10.027  20.928  -1.759  1.00 31.88           C  
ANISOU 4977  C5  NAG C   1     4490   4774   2848    516    584   -158       C  
HETATM 4978  C6  NAG C   1      10.412  21.075  -3.213  1.00 29.74           C  
ANISOU 4978  C6  NAG C   1     4248   4575   2475    580    629   -142       C  
HETATM 4979  C7  NAG C   1       8.321  22.620   2.994  1.00 35.63           C  
ANISOU 4979  C7  NAG C   1     4873   5057   3610    372    446    -82       C  
HETATM 4980  C8  NAG C   1       8.164  22.214   4.431  1.00 31.85           C  
ANISOU 4980  C8  NAG C   1     4370   4507   3223    313    414   -107       C  
HETATM 4981  N2  NAG C   1       8.902  21.727   2.191  1.00 27.29           N  
ANISOU 4981  N2  NAG C   1     3833   4017   2519    382    475   -124       N  
HETATM 4982  O3  NAG C   1       6.876  21.161   0.276  1.00 37.24           O  
ANISOU 4982  O3  NAG C   1     5112   5470   3570    434    406   -227       O  
HETATM 4983  O4  NAG C   1       7.892  19.893  -2.140  1.00 35.15           O  
ANISOU 4983  O4  NAG C   1     4895   5300   3158    497    476   -301       O  
HETATM 4984  O5  NAG C   1      10.685  21.983  -1.041  1.00 31.13           O  
ANISOU 4984  O5  NAG C   1     4384   4612   2834    514    614    -65       O  
HETATM 4985  O6  NAG C   1      10.033  22.356  -3.702  1.00 34.00           O  
ANISOU 4985  O6  NAG C   1     4795   5167   2957    634    634    -61       O  
HETATM 4986  O7  NAG C   1       7.942  23.703   2.581  1.00 36.06           O  
ANISOU 4986  O7  NAG C   1     4930   5149   3621    411    447    -24       O  
HETATM 4987  C1  NAG C   2       6.992  20.300  -3.198  1.00 36.33           C  
ANISOU 4987  C1  NAG C   2     5054   5564   3186    549    448   -308       C  
HETATM 4988  C2  NAG C   2       6.695  19.048  -4.012  1.00 40.09           C  
ANISOU 4988  C2  NAG C   2     5540   6100   3594    544    432   -420       C  
HETATM 4989  C3  NAG C   2       5.701  19.353  -5.130  1.00 43.15           C  
ANISOU 4989  C3  NAG C   2     5932   6618   3845    597    395   -442       C  
HETATM 4990  C4  NAG C   2       4.459  20.032  -4.572  1.00 43.58           C  
ANISOU 4990  C4  NAG C   2     5959   6700   3898    591    330   -426       C  
HETATM 4991  C5  NAG C   2       4.863  21.251  -3.742  1.00 45.69           C  
ANISOU 4991  C5  NAG C   2     6222   6897   4242    596    355   -308       C  
HETATM 4992  C6  NAG C   2       3.694  21.921  -3.059  1.00 50.96           C  
ANISOU 4992  C6  NAG C   2     6861   7578   4922    586    296   -290       C  
HETATM 4993  C7  NAG C   2       8.482  17.376  -4.068  1.00 42.98           C  
ANISOU 4993  C7  NAG C   2     5927   6366   4037    506    515   -486       C  
HETATM 4994  C8  NAG C   2       9.723  16.919  -4.762  1.00 41.58           C  
ANISOU 4994  C8  NAG C   2     5775   6172   3851    529    586   -485       C  
HETATM 4995  N2  NAG C   2       7.913  18.479  -4.560  1.00 38.94           N  
ANISOU 4995  N2  NAG C   2     5417   5927   3450    555    498   -428       N  
HETATM 4996  O3  NAG C   2       5.352  18.118  -5.745  1.00 43.77           O  
ANISOU 4996  O3  NAG C   2     6013   6746   3872    581    374   -563       O  
HETATM 4997  O4  NAG C   2       3.575  20.401  -5.626  1.00 53.46           O  
ANISOU 4997  O4  NAG C   2     7212   8079   5021    648    296   -437       O  
HETATM 4998  O5  NAG C   2       5.773  20.850  -2.704  1.00 37.90           O  
ANISOU 4998  O5  NAG C   2     5230   5792   3378    541    386   -302       O  
HETATM 4999  O6  NAG C   2       3.029  21.012  -2.192  1.00 68.44           O  
ANISOU 4999  O6  NAG C   2     9050   9758   7195    518    247   -376       O  
HETATM 5000  O7  NAG C   2       8.022  16.785  -3.092  1.00 47.31           O  
ANISOU 5000  O7  NAG C   2     6454   6863   4658    448    479   -534       O  
HETATM 5001  C1  NAG D   1     -19.933  34.667  74.864  1.00 33.89           C  
ANISOU 5001  C1  NAG D   1     4852   4716   3308    468    367   -251       C  
HETATM 5002  C2  NAG D   1     -21.423  34.583  74.467  1.00 33.67           C  
ANISOU 5002  C2  NAG D   1     4817   4627   3351    450    432   -214       C  
HETATM 5003  C3  NAG D   1     -22.256  35.634  75.209  1.00 36.71           C  
ANISOU 5003  C3  NAG D   1     5212   5018   3716    462    464   -260       C  
HETATM 5004  C4  NAG D   1     -21.960  35.641  76.703  1.00 33.72           C  
ANISOU 5004  C4  NAG D   1     4873   4717   3223    521    472   -275       C  
HETATM 5005  C5  NAG D   1     -20.458  35.753  76.933  1.00 30.66           C  
ANISOU 5005  C5  NAG D   1     4488   4387   2774    531    399   -316       C  
HETATM 5006  C6  NAG D   1     -20.063  35.692  78.390  1.00 36.33           C  
ANISOU 5006  C6  NAG D   1     5242   5193   3370    594    399   -332       C  
HETATM 5007  C7  NAG D   1     -22.186  33.825  72.267  1.00 38.02           C  
ANISOU 5007  C7  NAG D   1     5315   5068   4065    375    446   -154       C  
HETATM 5008  C8  NAG D   1     -22.329  34.160  70.811  1.00 34.53           C  
ANISOU 5008  C8  NAG D   1     4835   4568   3717    320    422   -165       C  
HETATM 5009  N2  NAG D   1     -21.592  34.748  73.031  1.00 32.04           N  
ANISOU 5009  N2  NAG D   1     4573   4355   3245    394    415   -215       N  
HETATM 5010  O3  NAG D   1     -23.639  35.358  75.013  1.00 37.61           O  
ANISOU 5010  O3  NAG D   1     5321   5086   3885    456    531   -216       O  
HETATM 5011  O4  NAG D   1     -22.612  36.764  77.287  1.00 40.97           O  
ANISOU 5011  O4  NAG D   1     5800   5639   4129    526    494   -332       O  
HETATM 5012  O5  NAG D   1     -19.808  34.651  76.289  1.00 36.26           O  
ANISOU 5012  O5  NAG D   1     5187   5088   3502    526    380   -259       O  
HETATM 5013  O6  NAG D   1     -20.510  34.476  78.977  1.00 40.43           O  
ANISOU 5013  O6  NAG D   1     5787   5730   3846    641    455   -245       O  
HETATM 5014  O7  NAG D   1     -22.576  32.764  72.730  1.00 37.42           O  
ANISOU 5014  O7  NAG D   1     5254   4996   3967    403    493    -94       O  
HETATM 5015  C1  NAG D   2     -23.539  36.374  78.327  1.00 47.59           C  
ANISOU 5015  C1  NAG D   2     6667   6499   4915    573    564   -294       C  
HETATM 5016  C2  NAG D   2     -23.890  37.606  79.172  1.00 52.02           C  
ANISOU 5016  C2  NAG D   2     7245   7086   5436    589    575   -368       C  
HETATM 5017  C3  NAG D   2     -24.959  37.263  80.208  1.00 64.42           C  
ANISOU 5017  C3  NAG D   2     8845   8674   6958    637    655   -328       C  
HETATM 5018  C4  NAG D   2     -26.153  36.581  79.556  1.00 63.07           C  
ANISOU 5018  C4  NAG D   2     8655   8435   6873    618    719   -253       C  
HETATM 5019  C5  NAG D   2     -25.685  35.389  78.731  1.00 58.02           C  
ANISOU 5019  C5  NAG D   2     8000   7774   6272    600    702   -187       C  
HETATM 5020  C6  NAG D   2     -26.806  34.734  77.963  1.00 74.53           C  
ANISOU 5020  C6  NAG D   2    10065   9796   8458    573    757   -124       C  
HETATM 5021  C7  NAG D   2     -22.059  39.222  79.403  1.00 53.13           C  
ANISOU 5021  C7  NAG D   2     7378   7284   5523    569    459   -522       C  
HETATM 5022  C8  NAG D   2     -20.864  39.631  80.213  1.00 57.25           C  
ANISOU 5022  C8  NAG D   2     7913   7885   5953    592    401   -593       C  
HETATM 5023  N2  NAG D   2     -22.711  38.140  79.832  1.00 52.41           N  
ANISOU 5023  N2  NAG D   2     7307   7203   5402    607    515   -438       N  
HETATM 5024  O3  NAG D   2     -25.385  38.465  80.836  1.00 59.71           O  
ANISOU 5024  O3  NAG D   2     8260   8089   6339    644    669   -400       O  
HETATM 5025  O4  NAG D   2     -27.060  36.142  80.561  1.00 70.70           O  
ANISOU 5025  O4  NAG D   2     9649   9421   7792    666    797   -209       O  
HETATM 5026  O5  NAG D   2     -24.722  35.826  77.762  1.00 52.87           O  
ANISOU 5026  O5  NAG D   2     7322   7106   5661    556    625   -231       O  
HETATM 5027  O6  NAG D   2     -27.338  35.622  76.989  1.00 80.49           O  
ANISOU 5027  O6  NAG D   2    10784  10496   9305    523    744   -163       O  
HETATM 5028  O7  NAG D   2     -22.408  39.837  78.401  1.00 62.32           O  
ANISOU 5028  O7  NAG D   2     8515   8380   6785    520    456   -538       O  
HETATM 5029  C   ACE A 401      17.519  34.807   4.984  1.00 71.76           C  
ANISOU 5029  C   ACE A 401     9317   9044   8906    442   1055    724       C  
HETATM 5030  O   ACE A 401      18.486  34.248   5.493  1.00 74.11           O  
ANISOU 5030  O   ACE A 401     9586   9303   9268    405   1059    692       O  
HETATM 5031  CH3 ACE A 401      17.715  35.961   4.050  1.00 81.33           C  
ANISOU 5031  CH3 ACE A 401    10544  10250  10108    493   1137    811       C  
HETATM 5032  C1  RET A 402      10.791  31.598  30.427  1.00 25.47           C  
ANISOU 5032  C1  RET A 402     3153   2961   3564   -175     51     12       C  
HETATM 5033  C2  RET A 402      11.586  32.131  31.642  1.00 29.71           C  
ANISOU 5033  C2  RET A 402     3654   3490   4143   -192     33    -12       C  
HETATM 5034  C3  RET A 402      11.856  31.175  32.784  1.00 25.06           C  
ANISOU 5034  C3  RET A 402     3056   2922   3543   -190     -3    -33       C  
HETATM 5035  C4  RET A 402      10.652  30.334  33.135  1.00 23.10           C  
ANISOU 5035  C4  RET A 402     2841   2690   3247   -181    -25    -34       C  
HETATM 5036  C5  RET A 402       9.956  29.756  31.950  1.00 22.27           C  
ANISOU 5036  C5  RET A 402     2765   2586   3109   -170     -6    -15       C  
HETATM 5037  C6  RET A 402      10.056  30.286  30.716  1.00 18.50           C  
ANISOU 5037  C6  RET A 402     2294   2100   2636   -166     26      4       C  
HETATM 5038  C7  RET A 402       9.309  29.756  29.587  1.00 22.52           C  
ANISOU 5038  C7  RET A 402     2832   2620   3107   -153     40     17       C  
HETATM 5039  C8  RET A 402       9.418  28.462  29.151  1.00 18.32           C  
ANISOU 5039  C8  RET A 402     2311   2097   2551   -144     43     14       C  
HETATM 5040  C9  RET A 402       8.714  27.802  28.076  1.00 22.32           C  
ANISOU 5040  C9  RET A 402     2844   2618   3018   -133     54     16       C  
HETATM 5041  C10 RET A 402       8.851  26.455  27.931  1.00 22.31           C  
ANISOU 5041  C10 RET A 402     2852   2622   3002   -128     55      5       C  
HETATM 5042  C11 RET A 402       8.200  25.619  26.964  1.00 24.81           C  
ANISOU 5042  C11 RET A 402     3192   2953   3281   -121     64     -4       C  
HETATM 5043  C12 RET A 402       8.485  24.350  26.572  1.00 20.90           C  
ANISOU 5043  C12 RET A 402     2706   2458   2777   -115     76    -16       C  
HETATM 5044  C13 RET A 402       9.593  23.466  26.906  1.00 21.29           C  
ANISOU 5044  C13 RET A 402     2746   2492   2852   -110     87    -17       C  
HETATM 5045  C14 RET A 402       9.502  22.169  26.550  1.00 18.12           C  
ANISOU 5045  C14 RET A 402     2359   2089   2438   -106     98    -34       C  
HETATM 5046  C15 RET A 402      10.456  21.190  26.730  1.00 20.01           C  
ANISOU 5046  C15 RET A 402     2591   2312   2698    -96    114    -34       C  
HETATM 5047  C16 RET A 402      11.731  31.422  29.225  1.00 30.15           C  
ANISOU 5047  C16 RET A 402     3741   3548   4168   -165     89     32       C  
HETATM 5048  C17 RET A 402       9.784  32.713  30.112  1.00 26.46           C  
ANISOU 5048  C17 RET A 402     3294   3076   3684   -176     61     24       C  
HETATM 5049  C18 RET A 402       9.013  28.646  32.327  1.00 23.06           C  
ANISOU 5049  C18 RET A 402     2890   2701   3171   -163    -24    -21       C  
HETATM 5050  C19 RET A 402       7.852  28.644  27.169  1.00 19.74           C  
ANISOU 5050  C19 RET A 402     2531   2301   2666   -126     65     30       C  
HETATM 5051  C20 RET A 402      10.839  24.046  27.528  1.00 19.88           C  
ANISOU 5051  C20 RET A 402     2538   2302   2714   -109     88     -2       C  
HETATM 5052  C1  NAG A 403      21.029  33.895   7.232  1.00 43.00           C  
ANISOU 5052  C1  NAG A 403     5550   5235   5552    306   1086    647       C  
HETATM 5053  C2  NAG A 403      20.695  35.305   7.718  1.00 55.71           C  
ANISOU 5053  C2  NAG A 403     7147   6803   7217    296   1100    686       C  
HETATM 5054  C3  NAG A 403      21.667  36.314   7.109  1.00 56.41           C  
ANISOU 5054  C3  NAG A 403     7221   6847   7364    312   1199    752       C  
HETATM 5055  C4  NAG A 403      23.104  35.902   7.398  1.00 61.28           C  
ANISOU 5055  C4  NAG A 403     7794   7425   8064    282   1229    732       C  
HETATM 5056  C5  NAG A 403      23.336  34.464   6.939  1.00 63.42           C  
ANISOU 5056  C5  NAG A 403     8082   7743   8271    295   1209    694       C  
HETATM 5057  C6  NAG A 403      24.713  33.943   7.281  1.00 63.16           C  
ANISOU 5057  C6  NAG A 403     8005   7677   8317    268   1232    671       C  
HETATM 5058  C7  NAG A 403      18.555  36.351   8.264  1.00 57.96           C  
ANISOU 5058  C7  NAG A 403     7460   7109   7451    304   1031    698       C  
HETATM 5059  C8  NAG A 403      17.165  36.656   7.796  1.00 53.93           C  
ANISOU 5059  C8  NAG A 403     6988   6650   6853    343   1004    719       C  
HETATM 5060  N2  NAG A 403      19.324  35.671   7.409  1.00 52.88           N  
ANISOU 5060  N2  NAG A 403     6826   6486   6780    326   1070    703       N  
HETATM 5061  O3  NAG A 403      21.413  37.606   7.647  1.00 58.95           O  
ANISOU 5061  O3  NAG A 403     7527   7120   7751    297   1214    783       O  
HETATM 5062  O4  NAG A 403      24.009  36.774   6.732  1.00 64.27           O  
ANISOU 5062  O4  NAG A 403     8160   7764   8496    298   1327    794       O  
HETATM 5063  O5  NAG A 403      22.387  33.585   7.569  1.00 55.87           O  
ANISOU 5063  O5  NAG A 403     7141   6824   7265    279   1117    634       O  
HETATM 5064  O6  NAG A 403      24.985  34.072   8.670  1.00 68.73           O  
ANISOU 5064  O6  NAG A 403     8661   8341   9111    213   1186    633       O  
HETATM 5065  O7  NAG A 403      18.964  36.701   9.372  1.00 52.72           O  
ANISOU 5065  O7  NAG A 403     6759   6393   6880    257   1017    677       O  
HETATM 5066  O1  DAO A 404      22.842  24.766  22.233  1.00 52.32           O  
ANISOU 5066  O1  DAO A 404     6424   6335   7119    -25    416    126       O  
HETATM 5067  O2  DAO A 404      23.051  26.864  22.948  1.00 59.74           O  
ANISOU 5067  O2  DAO A 404     7318   7259   8122    -60    407    132       O  
HETATM 5068  C1  DAO A 404      23.198  25.628  23.061  1.00 57.30           C  
ANISOU 5068  C1  DAO A 404     7017   6961   7795    -44    397    124       C  
HETATM 5069  C2  DAO A 404      23.871  25.155  24.365  1.00 51.37           C  
ANISOU 5069  C2  DAO A 404     6222   6216   7078    -46    358    106       C  
HETATM 5070  C3  DAO A 404      23.175  25.595  25.645  1.00 47.21           C  
ANISOU 5070  C3  DAO A 404     5690   5698   6548    -65    302     87       C  
HETATM 5071  C4  DAO A 404      23.580  24.770  26.853  1.00 44.40           C  
ANISOU 5071  C4  DAO A 404     5309   5360   6202    -56    261     73       C  
HETATM 5072  C5  DAO A 404      22.396  24.263  27.653  1.00 39.82           C  
ANISOU 5072  C5  DAO A 404     4764   4791   5576    -55    218     62       C  
HETATM 5073  C6  DAO A 404      22.727  22.997  28.421  1.00 42.91           C  
ANISOU 5073  C6  DAO A 404     5148   5195   5960    -31    197     60       C  
HETATM 5074  C7  DAO A 404      23.604  23.173  29.656  1.00 56.36           C  
ANISOU 5074  C7  DAO A 404     6797   6920   7700    -29    162     51       C  
HETATM 5075  C8  DAO A 404      24.241  21.847  30.064  1.00 51.69           C  
ANISOU 5075  C8  DAO A 404     6194   6339   7108      5    159     61       C  
HETATM 5076  C9  DAO A 404      24.971  21.865  31.399  1.00 57.87           C  
ANISOU 5076  C9  DAO A 404     6925   7153   7911     16    116     53       C  
HETATM 5077  C10 DAO A 404      25.564  20.503  31.744  1.00 62.87           C  
ANISOU 5077  C10 DAO A 404     7550   7796   8542     57    118     70       C  
HETATM 5078  C11 DAO A 404      25.656  20.244  33.241  1.00 58.56           C  
ANISOU 5078  C11 DAO A 404     6980   7286   7985     76     67     68       C  
HETATM 5079  C12 DAO A 404      26.276  18.896  33.589  1.00 69.87           C  
ANISOU 5079  C12 DAO A 404     8404   8728   9416    123     73     92       C  
HETATM 5080  C18 OLC A 405      23.506  31.646  38.141  1.00 57.19           C  
ANISOU 5080  C18 OLC A 405     6636   7148   7946   -222   -144   -240       C  
HETATM 5081  C10 OLC A 405      24.606  30.612  29.204  1.00 68.34           C  
ANISOU 5081  C10 OLC A 405     8174   8358   9434   -184    220     -1       C  
HETATM 5082  C9  OLC A 405      23.497  31.123  28.738  1.00 70.24           C  
ANISOU 5082  C9  OLC A 405     8462   8581   9644   -189    233     12       C  
HETATM 5083  C17 OLC A 405      23.935  30.381  37.439  1.00 56.60           C  
ANISOU 5083  C17 OLC A 405     6572   7077   7856   -189   -124   -196       C  
HETATM 5084  C11 OLC A 405      25.024  30.669  30.639  1.00 64.98           C  
ANISOU 5084  C11 OLC A 405     7702   7961   9028   -194    165    -41       C  
HETATM 5085  C8  OLC A 405      22.981  30.925  27.348  1.00 62.71           C  
ANISOU 5085  C8  OLC A 405     7558   7612   8655   -171    280     50       C  
HETATM 5086  C24 OLC A 405      24.112  30.051  16.930  1.00 68.50           C  
ANISOU 5086  C24 OLC A 405     8485   8319   9223      2    707    295       C  
HETATM 5087  C16 OLC A 405      23.650  30.353  35.962  1.00 51.89           C  
ANISOU 5087  C16 OLC A 405     6014   6433   7270   -192    -65   -157       C  
HETATM 5088  C12 OLC A 405      24.106  29.900  31.531  1.00 61.80           C  
ANISOU 5088  C12 OLC A 405     7333   7586   8562   -179    113    -48       C  
HETATM 5089  C7  OLC A 405      22.948  32.185  26.550  1.00 65.22           C  
ANISOU 5089  C7  OLC A 405     7877   7896   9006   -185    330     68       C  
HETATM 5090  C15 OLC A 405      24.037  29.051  35.318  1.00 56.39           C  
ANISOU 5090  C15 OLC A 405     6598   7007   7822   -158    -45   -119       C  
HETATM 5091  C13 OLC A 405      24.473  29.959  33.001  1.00 59.78           C  
ANISOU 5091  C13 OLC A 405     7033   7364   8314   -184     56    -86       C  
HETATM 5092  C6  OLC A 405      22.520  31.976  25.106  1.00 55.24           C  
ANISOU 5092  C6  OLC A 405     6661   6625   7702   -161    378    108       C  
HETATM 5093  C14 OLC A 405      23.727  28.968  33.848  1.00 53.57           C  
ANISOU 5093  C14 OLC A 405     6280   6610   7466   -159     12    -84       C  
HETATM 5094  C5  OLC A 405      23.073  32.999  24.155  1.00 62.36           C  
ANISOU 5094  C5  OLC A 405     7550   7494   8649   -166    444    136       C  
HETATM 5095  C4  OLC A 405      22.930  32.596  22.719  1.00 54.58           C  
ANISOU 5095  C4  OLC A 405     6606   6512   7621   -135    492    176       C  
HETATM 5096  C3  OLC A 405      23.929  33.229  21.765  1.00 52.55           C  
ANISOU 5096  C3  OLC A 405     6325   6227   7415   -133    565    206       C  
HETATM 5097  C2  OLC A 405      24.252  32.282  20.666  1.00 56.85           C  
ANISOU 5097  C2  OLC A 405     6894   6788   7919   -101    598    229       C  
HETATM 5098  C21 OLC A 405      25.120  32.346  17.194  1.00 70.93           C  
ANISOU 5098  C21 OLC A 405     8727   8562   9660    -32    770    329       C  
HETATM 5099  C1  OLC A 405      24.969  32.874  19.495  1.00 61.59           C  
ANISOU 5099  C1  OLC A 405     7488   7365   8548    -89    678    268       C  
HETATM 5100  C22 OLC A 405      25.062  31.084  16.363  1.00 76.32           C  
ANISOU 5100  C22 OLC A 405     9445   9277  10274      1    776    330       C  
HETATM 5101  O19 OLC A 405      25.339  34.011  19.378  1.00 68.86           O  
ANISOU 5101  O19 OLC A 405     8384   8252   9527   -104    718    284       O  
HETATM 5102  O25 OLC A 405      24.073  28.872  16.132  1.00 73.76           O  
ANISOU 5102  O25 OLC A 405     9184   9010   9830     30    717    290       O  
HETATM 5103  O23 OLC A 405      24.680  31.415  15.029  1.00 87.60           O  
ANISOU 5103  O23 OLC A 405    10917  10714  11651     32    829    371       O  
HETATM 5104  O20 OLC A 405      25.167  31.937  18.576  1.00 67.39           O  
ANISOU 5104  O20 OLC A 405     8248   8120   9238    -59    702    283       O  
HETATM 5105  C10 OLC A 406      -3.155  22.542  43.515  1.00 64.85           C  
ANISOU 5105  C10 OLC A 406     8348   8025   8265   -136    -75    -38       C  
HETATM 5106  C9  OLC A 406      -3.084  22.075  44.731  1.00 60.57           C  
ANISOU 5106  C9  OLC A 406     7817   7489   7709   -115    -68    -20       C  
HETATM 5107  C11 OLC A 406      -3.855  21.814  42.411  1.00 58.70           C  
ANISOU 5107  C11 OLC A 406     7570   7226   7506   -156    -55    -47       C  
HETATM 5108  C8  OLC A 406      -1.962  22.275  45.701  1.00 56.62           C  
ANISOU 5108  C8  OLC A 406     7314   7011   7187    -88    -86    -10       C  
HETATM 5109  C24 OLC A 406      -6.369  17.709  54.668  1.00 82.16           C  
ANISOU 5109  C24 OLC A 406    10692  10258  10266    117    144    216       C  
HETATM 5110  C12 OLC A 406      -4.800  22.636  41.597  1.00 48.60           C  
ANISOU 5110  C12 OLC A 406     6281   5953   6230   -177    -64    -66       C  
HETATM 5111  C7  OLC A 406      -2.398  22.863  47.002  1.00 65.60           C  
ANISOU 5111  C7  OLC A 406     8457   8170   8297    -74    -95    -10       C  
HETATM 5112  C15 OLC A 406      -6.924  21.799  38.441  1.00 61.54           C  
ANISOU 5112  C15 OLC A 406     7899   7590   7894   -228    -49   -120       C  
HETATM 5113  C13 OLC A 406      -5.365  21.862  40.421  1.00 48.92           C  
ANISOU 5113  C13 OLC A 406     6319   5983   6287   -195    -50    -81       C  
HETATM 5114  C6  OLC A 406      -3.789  22.426  47.438  1.00 70.77           C  
ANISOU 5114  C6  OLC A 406     9127   8812   8952    -78    -66     -1       C  
HETATM 5115  C14 OLC A 406      -6.350  22.615  39.574  1.00 55.56           C  
ANISOU 5115  C14 OLC A 406     7147   6836   7126   -211    -60    -99       C  
HETATM 5116  C5  OLC A 406      -4.073  22.628  48.902  1.00 65.60           C  
ANISOU 5116  C5  OLC A 406     8483   8179   8264    -53    -66      9       C  
HETATM 5117  C4  OLC A 406      -3.417  21.608  49.786  1.00 65.32           C  
ANISOU 5117  C4  OLC A 406     8459   8152   8207    -17    -53     41       C  
HETATM 5118  C3  OLC A 406      -3.805  21.710  51.246  1.00 71.30           C  
ANISOU 5118  C3  OLC A 406     9230   8935   8925     12    -48     55       C  
HETATM 5119  C2  OLC A 406      -3.315  20.547  52.048  1.00 77.60           C  
ANISOU 5119  C2  OLC A 406    10042   9738   9703     53    -26     96       C  
HETATM 5120  C21 OLC A 406      -4.880  19.603  53.892  1.00 80.71           C  
ANISOU 5120  C21 OLC A 406    10475  10130  10063     94     40    149       C  
HETATM 5121  C1  OLC A 406      -4.003  19.246  51.718  1.00 88.14           C  
ANISOU 5121  C1  OLC A 406    11391  11028  11068     50     26    125       C  
HETATM 5122  C22 OLC A 406      -5.366  18.776  55.060  1.00 79.17           C  
ANISOU 5122  C22 OLC A 406    10304   9935   9841    133     84    194       C  
HETATM 5123  O19 OLC A 406      -4.018  18.724  50.632  1.00 90.32           O  
ANISOU 5123  O19 OLC A 406    11662  11271  11384     26     39    119       O  
HETATM 5124  O25 OLC A 406      -6.775  16.926  55.788  1.00 79.77           O  
ANISOU 5124  O25 OLC A 406    10413   9954   9943    156    191    264       O  
HETATM 5125  O23 OLC A 406      -4.248  18.201  55.737  1.00 83.26           O  
ANISOU 5125  O23 OLC A 406    10828  10482  10324    182     78    227       O  
HETATM 5126  O20 OLC A 406      -4.609  18.720  52.781  1.00 91.43           O  
ANISOU 5126  O20 OLC A 406    11828  11447  11466     76     59    156       O  
HETATM 5127  C10 OLC A 407      15.767  39.373  28.135  1.00 42.86           C  
ANISOU 5127  C10 OLC A 407     5190   4932   6163   -251    324     72       C  
HETATM 5128  C9  OLC A 407      14.759  40.105  28.537  1.00 49.04           C  
ANISOU 5128  C9  OLC A 407     5990   5702   6940   -254    316     69       C  
HETATM 5129  C11 OLC A 407      16.698  38.538  28.956  1.00 49.74           C  
ANISOU 5129  C11 OLC A 407     6025   5828   7045   -266    284     32       C  
HETATM 5130  C8  OLC A 407      14.039  41.064  27.637  1.00 48.84           C  
ANISOU 5130  C8  OLC A 407     5993   5649   6916   -235    366    115       C  
HETATM 5131  C12 OLC A 407      16.862  37.150  28.440  1.00 41.11           C  
ANISOU 5131  C12 OLC A 407     4950   4772   5900   -242    271     48       C  
HETATM 5132  C7  OLC A 407      13.016  41.915  28.322  1.00 47.31           C  
ANISOU 5132  C7  OLC A 407     5811   5438   6728   -242    354    102       C  
HETATM 5133  C13 OLC A 407      17.964  36.356  29.121  1.00 44.88           C  
ANISOU 5133  C13 OLC A 407     5387   5270   6396   -252    243     17       C  
HETATM 5134  C10 OLC A 408      19.604  15.282  25.276  1.00 51.76           C  
ANISOU 5134  C10 OLC A 408     6516   6234   6918     54    331     28       C  
HETATM 5135  C9  OLC A 408      20.412  14.673  24.442  1.00 51.40           C  
ANISOU 5135  C9  OLC A 408     6469   6176   6885     72    373     29       C  
HETATM 5136  C11 OLC A 408      19.907  15.574  26.712  1.00 56.54           C  
ANISOU 5136  C11 OLC A 408     7089   6848   7544     59    293     46       C  
HETATM 5137  C8  OLC A 408      20.154  14.454  22.983  1.00 48.13           C  
ANISOU 5137  C8  OLC A 408     6086   5759   6444     69    411      8       C  
HETATM 5138  C12 OLC A 408      19.660  16.996  27.096  1.00 40.14           C  
ANISOU 5138  C12 OLC A 408     4995   4793   5464     37    258     48       C  
HETATM 5139  C7  OLC A 408      21.272  14.933  22.114  1.00 61.83           C  
ANISOU 5139  C7  OLC A 408     7800   7499   8193     80    444     22       C  
HETATM 5140  C13 OLC A 408      20.113  17.353  28.502  1.00 41.16           C  
ANISOU 5140  C13 OLC A 408     5088   4938   5614     42    219     61       C  
HETATM 5141  C6  OLC A 408      21.038  14.753  20.620  1.00 53.07           C  
ANISOU 5141  C6  OLC A 408     6722   6393   7048     82    483      2       C  
HETATM 5142  C14 OLC A 408      21.607  17.323  28.717  1.00 49.26           C  
ANISOU 5142  C14 OLC A 408     6065   5970   6679     63    227     76       C  
HETATM 5143  C5  OLC A 408      22.235  15.106  19.761  1.00 50.31           C  
ANISOU 5143  C5  OLC A 408     6353   6046   6715     98    525     19       C  
HETATM 5144  C10 OLC A 409      24.190  22.446  45.947  1.00 62.38           C  
ANISOU 5144  C10 OLC A 409     7316   8211   8176    190   -413    -73       C  
HETATM 5145  C9  OLC A 409      24.033  21.503  46.847  1.00 68.18           C  
ANISOU 5145  C9  OLC A 409     8066   8982   8858    245   -428    -38       C  
HETATM 5146  C11 OLC A 409      24.307  22.297  44.462  1.00 63.38           C  
ANISOU 5146  C11 OLC A 409     7456   8272   8354    164   -359    -56       C  
HETATM 5147  C8  OLC A 409      23.835  21.819  48.295  1.00 52.81           C  
ANISOU 5147  C8  OLC A 409     6108   7103   6855    267   -481    -60       C  
HETATM 5148  C12 OLC A 409      24.614  23.588  43.768  1.00 44.77           C  
ANISOU 5148  C12 OLC A 409     5069   5891   6051    106   -354   -101       C  
HETATM 5149  C7  OLC A 409      23.891  20.648  49.223  1.00 54.63           C  
ANISOU 5149  C7  OLC A 409     6350   7379   7029    340   -492    -10       C  
HETATM 5150  C13 OLC A 409      24.546  23.506  42.250  1.00 40.99           C  
ANISOU 5150  C13 OLC A 409     4614   5346   5613     82   -296    -82       C  
HETATM 5151  C6  OLC A 409      23.934  21.075  50.682  1.00 43.38           C  
ANISOU 5151  C6  OLC A 409     4900   6036   5545    365   -551    -39       C  
HETATM 5152  C5  OLC A 409      23.465  20.042  51.668  1.00 52.07           C  
ANISOU 5152  C5  OLC A 409     6037   7170   6576    433   -553     15       C  
HETATM 5153  C4  OLC A 409      23.044  20.621  52.998  1.00 46.55           C  
ANISOU 5153  C4  OLC A 409     5337   6538   5812    446   -602    -16       C  
HETATM 5154  C3  OLC A 409      22.544  19.590  53.993  1.00 59.79           C  
ANISOU 5154  C3  OLC A 409     7054   8248   7416    517   -597     44       C  
HETATM 5155  C2  OLC A 409      22.317  20.169  55.353  1.00 66.78           C  
ANISOU 5155  C2  OLC A 409     7929   9213   8231    537   -650     10       C  
HETATM 5156  C1  PLM A 410      12.610   2.142  53.844  1.00 67.68           C  
ANISOU 5156  C1  PLM A 410     8788   8348   8580    921    419    931       C  
HETATM 5157  O2  PLM A 410      12.444   1.125  54.574  1.00 80.35           O  
ANISOU 5157  O2  PLM A 410    10419   9926  10183    985    483   1008       O  
HETATM 5158  C2  PLM A 410      13.965   2.213  53.096  1.00 55.80           C  
ANISOU 5158  C2  PLM A 410     7241   6864   7095    928    386    913       C  
HETATM 5159  C3  PLM A 410      13.886   2.682  51.662  1.00 71.44           C  
ANISOU 5159  C3  PLM A 410     9212   8803   9130    841    374    835       C  
HETATM 5160  C4  PLM A 410      15.241   2.986  51.034  1.00 66.88           C  
ANISOU 5160  C4  PLM A 410     8589   8261   8563    848    332    814       C  
HETATM 5161  C5  PLM A 410      15.125   3.286  49.547  1.00 76.61           C  
ANISOU 5161  C5  PLM A 410     9817   9442   9850    767    335    744       C  
HETATM 5162  C6  PLM A 410      16.438   3.658  48.864  1.00 68.12           C  
ANISOU 5162  C6  PLM A 410     8695   8399   8788    769    296    721       C  
HETATM 5163  C7  PLM A 410      16.484   3.187  47.417  1.00 73.09           C  
ANISOU 5163  C7  PLM A 410     9333   8952   9485    724    341    688       C  
HETATM 5164  C8  PLM A 410      17.434   3.969  46.517  1.00 60.68           C  
ANISOU 5164  C8  PLM A 410     7720   7411   7925    693    295    639       C  
HETATM 5165  C9  PLM A 410      17.832   3.183  45.272  1.00 59.64           C  
ANISOU 5165  C9  PLM A 410     7594   7212   7856    680    350    629       C  
HETATM 5166  CA  PLM A 410      18.578   4.011  44.235  1.00 57.03           C  
ANISOU 5166  CA  PLM A 410     7227   6901   7539    640    312    576       C  
HETATM 5167  CB  PLM A 410      17.643   4.821  43.317  1.00 73.99           C  
ANISOU 5167  CB  PLM A 410     9392   9028   9693    555    299    508       C  
HETATM 5168  CC  PLM A 410      18.393   5.673  42.283  1.00 67.70           C  
ANISOU 5168  CC  PLM A 410     8562   8253   8909    518    267    461       C  
HETATM 5169  CD  PLM A 410      17.480   6.320  41.238  1.00 63.33           C  
ANISOU 5169  CD  PLM A 410     8027   7671   8363    442    265    400       C  
HETATM 5170  CE  PLM A 410      18.142   7.449  40.447  1.00 60.62           C  
ANISOU 5170  CE  PLM A 410     7650   7362   8021    408    224    358       C  
HETATM 5171  CF  PLM A 410      19.074   6.962  39.338  1.00 64.85           C  
ANISOU 5171  CF  PLM A 410     8173   7870   8596    413    259    353       C  
HETATM 5172  CG  PLM A 410      19.620   8.098  38.461  1.00 54.39           C  
ANISOU 5172  CG  PLM A 410     6818   6574   7275    375    227    312       C  
HETATM 5173  C8  OLC A 411      24.895  34.808  44.588  1.00 68.45           C  
ANISOU 5173  C8  OLC A 411     7836   8786   9385   -290   -397   -558       C  
HETATM 5174  C7  OLC A 411      24.953  35.167  46.040  1.00 67.94           C  
ANISOU 5174  C7  OLC A 411     7739   8784   9288   -289   -459   -623       C  
HETATM 5175  C6  OLC A 411      25.448  34.037  46.929  1.00 55.82           C  
ANISOU 5175  C6  OLC A 411     6185   7335   7691   -236   -514   -614       C  
HETATM 5176  C5  OLC A 411      25.306  34.282  48.415  1.00 70.89           C  
ANISOU 5176  C5  OLC A 411     8075   9314   9547   -225   -577   -671       C  
HETATM 5177  C4  OLC A 411      26.197  35.359  48.984  1.00 62.41           C  
ANISOU 5177  C4  OLC A 411     6920   8267   8525   -264   -607   -763       C  
HETATM 5178  C3  OLC A 411      26.296  35.323  50.503  1.00 55.50           C  
ANISOU 5178  C3  OLC A 411     6017   7486   7585   -240   -680   -818       C  
HETATM 5179  C2  OLC A 411      24.959  35.447  51.170  1.00 66.82           C  
ANISOU 5179  C2  OLC A 411     7519   8919   8951   -230   -688   -816       C  
HETATM 5180  C1  OLC A 411      24.893  34.773  52.513  1.00 63.64           C  
ANISOU 5180  C1  OLC A 411     7116   8613   8451   -176   -751   -824       C  
HETATM 5181  O19 OLC A 411      23.895  33.897  52.567  1.00 74.76           O  
ANISOU 5181  O19 OLC A 411     8599  10014   9791   -135   -738   -754       O  
HETATM 5182  O20 OLC A 411      25.632  34.986  53.436  1.00 66.11           O  
ANISOU 5182  O20 OLC A 411     7368   9002   8749   -169   -806   -886       O  
HETATM 5183  C18 OLC A 412      -7.320  25.172  37.271  1.00 48.63           C  
ANISOU 5183  C18 OLC A 412     6242   6006   6230   -218   -100   -118       C  
HETATM 5184  C10 OLC A 412      -6.315  26.343  46.419  1.00 62.69           C  
ANISOU 5184  C10 OLC A 412     8078   7796   7946   -138   -103    -72       C  
HETATM 5185  C9  OLC A 412      -6.902  25.451  47.177  1.00 67.41           C  
ANISOU 5185  C9  OLC A 412     8687   8391   8535   -127    -81    -57       C  
HETATM 5186  C17 OLC A 412      -6.766  26.366  38.010  1.00 50.89           C  
ANISOU 5186  C17 OLC A 412     6531   6291   6515   -207   -110   -104       C  
HETATM 5187  C11 OLC A 412      -5.810  26.083  45.033  1.00 64.06           C  
ANISOU 5187  C11 OLC A 412     8242   7959   8140   -151   -106    -74       C  
HETATM 5188  C8  OLC A 412      -7.552  25.661  48.510  1.00 53.72           C  
ANISOU 5188  C8  OLC A 412     6965   6669   6778   -112    -72    -53       C  
HETATM 5189  C24 OLC A 412      -5.995  27.199  58.153  1.00 65.47           C  
ANISOU 5189  C24 OLC A 412     8531   8401   7946     98   -118    -65       C  
HETATM 5190  C16 OLC A 412      -6.917  26.296  39.507  1.00 49.65           C  
ANISOU 5190  C16 OLC A 412     6381   6126   6359   -203   -107    -99       C  
HETATM 5191  C12 OLC A 412      -6.592  26.843  44.011  1.00 64.14           C  
ANISOU 5191  C12 OLC A 412     8241   7964   8164   -168   -109    -85       C  
HETATM 5192  C7  OLC A 412      -7.728  24.371  49.253  1.00 59.45           C  
ANISOU 5192  C7  OLC A 412     7706   7389   7494    -94    -43    -26       C  
HETATM 5193  C15 OLC A 412      -6.421  27.538  40.193  1.00 51.51           C  
ANISOU 5193  C15 OLC A 412     6616   6363   6592   -194   -119    -95       C  
HETATM 5194  C13 OLC A 412      -6.115  26.708  42.578  1.00 59.65           C  
ANISOU 5194  C13 OLC A 412     7664   7390   7609   -179   -112    -87       C  
HETATM 5195  C6  OLC A 412      -8.040  24.531  50.734  1.00 54.44           C  
ANISOU 5195  C6  OLC A 412     7085   6773   6826    -69    -34    -17       C  
HETATM 5196  C14 OLC A 412      -6.820  27.654  41.639  1.00 61.26           C  
ANISOU 5196  C14 OLC A 412     7857   7597   7820   -188   -117    -94       C  
HETATM 5197  C5  OLC A 412      -7.372  23.504  51.619  1.00 56.48           C  
ANISOU 5197  C5  OLC A 412     7359   7041   7060    -37    -21     14       C  
HETATM 5198  C4  OLC A 412      -7.574  23.747  53.088  1.00 48.14           C  
ANISOU 5198  C4  OLC A 412     6318   6013   5960     -6    -16     22       C  
HETATM 5199  C3  OLC A 412      -6.388  23.383  53.969  1.00 50.96           C  
ANISOU 5199  C3  OLC A 412     6682   6402   6277     32    -30     39       C  
HETATM 5200  C2  OLC A 412      -6.601  23.813  55.389  1.00 57.64           C  
ANISOU 5200  C2  OLC A 412     7543   7285   7074     63    -32     40       C  
HETATM 5201  C21 OLC A 412      -6.320  24.690  58.147  1.00 65.60           C  
ANISOU 5201  C21 OLC A 412     8573   8388   7965    133    -54     30       C  
HETATM 5202  C1  OLC A 412      -5.438  23.532  56.300  1.00 64.75           C  
ANISOU 5202  C1  OLC A 412     8447   8228   7926    105    -52     53       C  
HETATM 5203  C22 OLC A 412      -6.039  25.925  58.971  1.00 67.98           C  
ANISOU 5203  C22 OLC A 412     8870   8734   8225    141    -90    -14       C  
HETATM 5204  O19 OLC A 412      -4.782  22.524  56.303  1.00 72.04           O  
ANISOU 5204  O19 OLC A 412     9375   9151   8847    128    -42     86       O  
HETATM 5205  O25 OLC A 412      -5.844  28.351  58.979  1.00 68.64           O  
ANISOU 5205  O25 OLC A 412     8929   8837   8313    103   -144   -111       O  
HETATM 5206  O23 OLC A 412      -7.025  26.032  59.996  1.00 64.22           O  
ANISOU 5206  O23 OLC A 412     8416   8272   7715    162    -62     -6       O  
HETATM 5207  O20 OLC A 412      -5.262  24.513  57.179  1.00 71.42           O  
ANISOU 5207  O20 OLC A 412     9291   9116   8731    118    -79     25       O  
HETATM 5208  C8  OLC A 413      -5.826  22.333  30.719  1.00 56.86           C  
ANISOU 5208  C8  OLC A 413     7278   7099   7228   -233    -84   -196       C  
HETATM 5209  C7  OLC A 413      -5.859  22.693  29.270  1.00 46.57           C  
ANISOU 5209  C7  OLC A 413     5970   5831   5893   -223    -92   -205       C  
HETATM 5210  C6  OLC A 413      -5.046  21.765  28.378  1.00 52.99           C  
ANISOU 5210  C6  OLC A 413     6792   6641   6702   -224    -76   -223       C  
HETATM 5211  C5  OLC A 413      -5.135  22.099  26.910  1.00 62.00           C  
ANISOU 5211  C5  OLC A 413     7929   7824   7804   -212    -84   -234       C  
HETATM 5212  C4  OLC A 413      -4.453  21.107  26.003  1.00 65.06           C  
ANISOU 5212  C4  OLC A 413     8326   8211   8184   -214    -68   -259       C  
HETATM 5213  C3  OLC A 413      -4.487  21.490  24.535  1.00 56.49           C  
ANISOU 5213  C3  OLC A 413     7238   7173   7052   -196    -74   -268       C  
HETATM 5214  C2  OLC A 413      -5.878  21.686  24.025  1.00 61.32           C  
ANISOU 5214  C2  OLC A 413     7832   7831   7635   -197    -99   -294       C  
HETATM 5215  C1  OLC A 413      -5.927  22.318  22.663  1.00 74.37           C  
ANISOU 5215  C1  OLC A 413     9483   9539   9234   -170   -108   -290       C  
HETATM 5216  O19 OLC A 413      -5.160  21.663  21.798  1.00 63.55           O  
ANISOU 5216  O19 OLC A 413     8124   8173   7847   -166    -93   -308       O  
HETATM 5217  O20 OLC A 413      -6.558  23.301  22.376  1.00 77.30           O  
ANISOU 5217  O20 OLC A 413     9845   9946   9579   -150   -126   -270       O  
HETATM 5218  C18 OLC A 414      -8.726  40.318  42.399  1.00 60.78           C  
ANISOU 5218  C18 OLC A 414     7760   7423   7909   -154    -64   -131       C  
HETATM 5219  C10 OLC A 414     -10.264  41.569  50.451  1.00 61.21           C  
ANISOU 5219  C10 OLC A 414     7862   7512   7883   -149    -68   -320       C  
HETATM 5220  C9  OLC A 414     -10.381  42.277  51.552  1.00 44.61           C  
ANISOU 5220  C9  OLC A 414     5765   5408   5775   -147    -61   -360       C  
HETATM 5221  C17 OLC A 414      -9.283  39.915  43.742  1.00 56.49           C  
ANISOU 5221  C17 OLC A 414     7224   6894   7344   -156    -73   -155       C  
HETATM 5222  C11 OLC A 414     -11.095  41.689  49.210  1.00 43.28           C  
ANISOU 5222  C11 OLC A 414     5585   5223   5638   -144    -51   -279       C  
HETATM 5223  C8  OLC A 414      -9.456  42.161  52.723  1.00 53.56           C  
ANISOU 5223  C8  OLC A 414     6903   6570   6879   -151    -83   -405       C  
HETATM 5224  C24 OLC A 414      -3.683  35.734  60.137  1.00 83.43           C  
ANISOU 5224  C24 OLC A 414    10711  10765  10222      3   -290   -459       C  
HETATM 5225  C16 OLC A 414      -8.261  39.746  44.842  1.00 56.94           C  
ANISOU 5225  C16 OLC A 414     7285   6956   7395   -169    -87   -189       C  
HETATM 5226  C12 OLC A 414     -11.585  40.379  48.666  1.00 43.83           C  
ANISOU 5226  C12 OLC A 414     5653   5316   5683   -139    -59   -242       C  
HETATM 5227  C7  OLC A 414     -10.147  41.915  54.030  1.00 40.99           C  
ANISOU 5227  C7  OLC A 414     5327   5005   5242   -134    -79   -421       C  
HETATM 5228  C15 OLC A 414      -8.832  39.226  46.142  1.00 55.67           C  
ANISOU 5228  C15 OLC A 414     7134   6815   7204   -165    -95   -207       C  
HETATM 5229  C13 OLC A 414     -10.535  39.501  48.001  1.00 42.55           C  
ANISOU 5229  C13 OLC A 414     5487   5165   5514   -149    -80   -230       C  
HETATM 5230  C6  OLC A 414      -9.270  41.201  55.046  1.00 51.09           C  
ANISOU 5230  C6  OLC A 414     6611   6330   6470   -128   -108   -444       C  
HETATM 5231  C14 OLC A 414      -9.935  40.072  46.736  1.00 52.82           C  
ANISOU 5231  C14 OLC A 414     6776   6443   6848   -156    -77   -216       C  
HETATM 5232  C5  OLC A 414      -7.851  41.717  55.095  1.00 59.90           C  
ANISOU 5232  C5  OLC A 414     7710   7448   7601   -145   -132   -487       C  
HETATM 5233  C4  OLC A 414      -6.975  41.034  56.112  1.00 66.86           C  
ANISOU 5233  C4  OLC A 414     8592   8382   8429   -134   -165   -510       C  
HETATM 5234  C3  OLC A 414      -5.557  41.576  56.181  1.00 71.23           C  
ANISOU 5234  C3  OLC A 414     9122   8941   9000   -153   -191   -559       C  
HETATM 5235  C2  OLC A 414      -4.788  41.033  57.348  1.00 78.47           C  
ANISOU 5235  C2  OLC A 414    10038   9920   9859   -137   -225   -588       C  
HETATM 5236  C21 OLC A 414      -3.956  37.621  58.469  1.00 78.14           C  
ANISOU 5236  C21 OLC A 414    10017  10000   9674    -66   -271   -501       C  
HETATM 5237  C1  OLC A 414      -4.489  39.563  57.243  1.00 84.45           C  
ANISOU 5237  C1  OLC A 414    10800  10710  10576   -117   -241   -537       C  
HETATM 5238  C22 OLC A 414      -3.623  37.226  59.890  1.00 82.09           C  
ANISOU 5238  C22 OLC A 414    10524  10566  10099    -32   -294   -520       C  
HETATM 5239  O19 OLC A 414      -4.576  38.912  56.236  1.00 82.19           O  
ANISOU 5239  O19 OLC A 414    10514  10403  10311   -121   -232   -488       O  
HETATM 5240  O25 OLC A 414      -2.603  35.050  59.508  1.00 79.37           O  
ANISOU 5240  O25 OLC A 414    10178  10258   9722      2   -312   -438       O  
HETATM 5241  O23 OLC A 414      -2.329  37.722  60.226  1.00 81.68           O  
ANISOU 5241  O23 OLC A 414    10444  10547  10046    -40   -333   -576       O  
HETATM 5242  O20 OLC A 414      -4.119  39.055  58.415  1.00 88.40           O  
ANISOU 5242  O20 OLC A 414    11307  11268  11014    -92   -264   -554       O  
HETATM 5243  C10 OLC A 415      -6.367  34.700  28.991  1.00 64.32           C  
ANISOU 5243  C10 OLC A 415     8200   8085   8156    -66    -75     55       C  
HETATM 5244  C9  OLC A 415      -6.290  34.651  27.689  1.00 49.35           C  
ANISOU 5244  C9  OLC A 415     6305   6218   6228    -44    -69     71       C  
HETATM 5245  C11 OLC A 415      -6.033  33.574  29.919  1.00 53.38           C  
ANISOU 5245  C11 OLC A 415     6816   6686   6780    -97    -88     20       C  
HETATM 5246  C8  OLC A 415      -6.802  35.683  26.738  1.00 51.97           C  
ANISOU 5246  C8  OLC A 415     6636   6571   6541     -6    -56    110       C  
HETATM 5247  C12 OLC A 415      -6.160  33.951  31.361  1.00 59.90           C  
ANISOU 5247  C12 OLC A 415     7641   7483   7636   -112    -92     10       C  
HETATM 5248  C7  OLC A 415      -6.422  35.399  25.321  1.00 51.71           C  
ANISOU 5248  C7  OLC A 415     6608   6572   6467     17    -48    125       C  
HETATM 5249  C13 OLC A 415      -6.106  32.780  32.323  1.00 55.32           C  
ANISOU 5249  C13 OLC A 415     7062   6898   7058   -136   -106    -20       C  
HETATM 5250  C6  OLC A 415      -7.204  36.218  24.309  1.00 42.60           C  
ANISOU 5250  C6  OLC A 415     5451   5457   5279     62    -42    162       C  
HETATM 5251  C14 OLC A 415      -6.102  33.177  33.787  1.00 43.60           C  
ANISOU 5251  C14 OLC A 415     5578   5388   5598   -147   -108    -29       C  
HETATM 5252  C5  OLC A 415      -6.943  35.861  22.864  1.00 46.45           C  
ANISOU 5252  C5  OLC A 415     5944   5990   5714     90    -38    175       C  
HETATM 5253  C4  OLC A 415      -7.852  36.571  21.896  1.00 47.26           C  
ANISOU 5253  C4  OLC A 415     6041   6143   5773    140    -38    210       C  
HETATM 5254  C3  OLC A 415      -7.702  36.138  20.448  1.00 51.81           C  
ANISOU 5254  C3  OLC A 415     6622   6778   6286    170    -39    217       C  
HETATM 5255  C2  OLC A 415      -8.522  36.975  19.510  1.00 61.49           C  
ANISOU 5255  C2  OLC A 415     7842   8055   7466    228    -37    262       C  
HETATM 5256  C   ACE B 401     -13.341  22.043  70.892  1.00 34.48           C  
ANISOU 5256  C   ACE B 401     4919   4694   3487    581    378    354       C  
HETATM 5257  O   ACE B 401     -12.321  22.247  70.221  1.00 35.97           O  
ANISOU 5257  O   ACE B 401     5086   4891   3689    561    317    323       O  
HETATM 5258  CH3 ACE B 401     -13.321  21.200  72.136  1.00 37.23           C  
ANISOU 5258  CH3 ACE B 401     5303   5082   3760    659    428    424       C  
HETATM 5259  C1  RET B 402     -19.775  24.889  44.947  1.00 25.73           C  
ANISOU 5259  C1  RET B 402     3251   3091   3432   -254     59   -136       C  
HETATM 5260  C2  RET B 402     -18.944  24.406  43.737  1.00 30.47           C  
ANISOU 5260  C2  RET B 402     3851   3695   4032   -266     37   -149       C  
HETATM 5261  C3  RET B 402     -18.564  25.449  42.708  1.00 37.62           C  
ANISOU 5261  C3  RET B 402     4749   4626   4918   -258     -2   -155       C  
HETATM 5262  C4  RET B 402     -19.791  26.204  42.265  1.00 25.04           C  
ANISOU 5262  C4  RET B 402     3123   3058   3332   -257    -12   -165       C  
HETATM 5263  C5  RET B 402     -20.593  26.741  43.416  1.00 18.73           C  
ANISOU 5263  C5  RET B 402     2324   2254   2539   -246      8   -154       C  
HETATM 5264  C6  RET B 402     -20.578  26.168  44.637  1.00 22.26           C  
ANISOU 5264  C6  RET B 402     2790   2678   2990   -246     40   -142       C  
HETATM 5265  C7  RET B 402     -21.252  26.769  45.774  1.00 22.29           C  
ANISOU 5265  C7  RET B 402     2798   2679   2992   -231     60   -130       C  
HETATM 5266  C8  RET B 402     -21.182  28.081  46.122  1.00 20.13           C  
ANISOU 5266  C8  RET B 402     2533   2416   2701   -210     47   -123       C  
HETATM 5267  C9  RET B 402     -21.861  28.741  47.220  1.00 24.60           C  
ANISOU 5267  C9  RET B 402     3104   2980   3264   -195     67   -115       C  
HETATM 5268  C10 RET B 402     -21.740  30.083  47.358  1.00 21.39           C  
ANISOU 5268  C10 RET B 402     2702   2580   2844   -176     53   -114       C  
HETATM 5269  C11 RET B 402     -22.379  30.907  48.343  1.00 19.24           C  
ANISOU 5269  C11 RET B 402     2435   2308   2568   -159     72   -110       C  
HETATM 5270  C12 RET B 402     -22.137  32.193  48.717  1.00 21.28           C  
ANISOU 5270  C12 RET B 402     2705   2565   2814   -140     64   -112       C  
HETATM 5271  C13 RET B 402     -21.059  33.110  48.375  1.00 20.74           C  
ANISOU 5271  C13 RET B 402     2652   2494   2733   -132     39   -115       C  
HETATM 5272  C14 RET B 402     -21.166  34.409  48.739  1.00 19.28           C  
ANISOU 5272  C14 RET B 402     2472   2305   2547   -116     41   -120       C  
HETATM 5273  C15 RET B 402     -20.219  35.408  48.524  1.00 19.09           C  
ANISOU 5273  C15 RET B 402     2462   2273   2520   -110     24   -126       C  
HETATM 5274  C16 RET B 402     -20.714  23.715  45.231  1.00 22.76           C  
ANISOU 5274  C16 RET B 402     2859   2696   3091   -275     98   -143       C  
HETATM 5275  C17 RET B 402     -18.855  25.089  46.162  1.00 20.49           C  
ANISOU 5275  C17 RET B 402     2626   2416   2742   -232     68   -111       C  
HETATM 5276  C18 RET B 402     -21.521  27.850  42.997  1.00 22.18           C  
ANISOU 5276  C18 RET B 402     2734   2716   2976   -235     -7   -156       C  
HETATM 5277  C19 RET B 402     -22.702  27.904  48.154  1.00 18.92           C  
ANISOU 5277  C19 RET B 402     2381   2248   2559   -200    109   -109       C  
HETATM 5278  C20 RET B 402     -19.831  32.571  47.687  1.00 23.62           C  
ANISOU 5278  C20 RET B 402     3028   2859   3089   -144     15   -115       C  
HETATM 5279  C1  NAG B 403      -9.342  22.872  68.068  1.00 36.82           C  
ANISOU 5279  C1  NAG B 403     5122   5013   3853    495    149    232       C  
HETATM 5280  C2  NAG B 403      -9.714  21.460  67.654  1.00 40.44           C  
ANISOU 5280  C2  NAG B 403     5592   5414   4360    501    212    305       C  
HETATM 5281  C3  NAG B 403      -8.785  20.460  68.345  1.00 38.87           C  
ANISOU 5281  C3  NAG B 403     5409   5256   4104    569    218    364       C  
HETATM 5282  C4  NAG B 403      -7.330  20.786  68.027  1.00 43.20           C  
ANISOU 5282  C4  NAG B 403     5932   5847   4634    572    143    330       C  
HETATM 5283  C5  NAG B 403      -7.024  22.250  68.348  1.00 43.08           C  
ANISOU 5283  C5  NAG B 403     5901   5888   4580    556     78    249       C  
HETATM 5284  C6  NAG B 403      -5.647  22.679  67.898  1.00 42.45           C  
ANISOU 5284  C6  NAG B 403     5789   5841   4497    546      4    206       C  
HETATM 5285  C7  NAG B 403     -11.898  20.524  67.069  1.00 40.01           C  
ANISOU 5285  C7  NAG B 403     5548   5243   4409    457    330    357       C  
HETATM 5286  C8  NAG B 403     -13.316  20.294  67.502  1.00 40.04           C  
ANISOU 5286  C8  NAG B 403     5568   5215   4431    456    402    383       C  
HETATM 5287  N2  NAG B 403     -11.109  21.163  67.942  1.00 34.30           N  
ANISOU 5287  N2  NAG B 403     4832   4596   3603    497    283    335       N  
HETATM 5288  O3  NAG B 403      -9.099  19.137  67.930  1.00 44.19           O  
ANISOU 5288  O3  NAG B 403     6094   5868   4830    573    282    432       O  
HETATM 5289  O4  NAG B 403      -6.475  19.961  68.815  1.00 45.90           O  
ANISOU 5289  O4  NAG B 403     6287   6240   4912    644    144    384       O  
HETATM 5290  O5  NAG B 403      -7.969  23.130  67.709  1.00 38.10           O  
ANISOU 5290  O5  NAG B 403     5261   5209   4005    494     82    201       O  
HETATM 5291  O6  NAG B 403      -5.454  22.467  66.507  1.00 42.30           O  
ANISOU 5291  O6  NAG B 403     5749   5758   4565    493      1    201       O  
HETATM 5292  O7  NAG B 403     -11.477  20.131  65.985  1.00 33.80           O  
ANISOU 5292  O7  NAG B 403     4743   4418   3681    423    316    353       O  
HETATM 5293  C10 OLC B 404     -34.170  34.161  30.943  1.00 55.90           C  
ANISOU 5293  C10 OLC B 404     6376   7726   7137     53   -347   -212       C  
HETATM 5294  C9  OLC B 404     -33.119  34.174  30.166  1.00 56.92           C  
ANISOU 5294  C9  OLC B 404     6543   7861   7224     63   -360   -201       C  
HETATM 5295  C11 OLC B 404     -34.302  33.760  32.379  1.00 47.14           C  
ANISOU 5295  C11 OLC B 404     5282   6545   6085     10   -304   -223       C  
HETATM 5296  C8  OLC B 404     -33.148  34.846  28.828  1.00 61.89           C  
ANISOU 5296  C8  OLC B 404     7156   8564   7795    120   -396   -175       C  
HETATM 5297  C12 OLC B 404     -35.161  34.719  33.143  1.00 52.66           C  
ANISOU 5297  C12 OLC B 404     5963   7233   6812     41   -280   -189       C  
HETATM 5298  C7  OLC B 404     -33.530  33.951  27.689  1.00 65.82           C  
ANISOU 5298  C7  OLC B 404     7606   9145   8259    110   -443   -230       C  
HETATM 5299  C15 OLC B 404     -37.209  34.653  36.439  1.00 63.77           C  
ANISOU 5299  C15 OLC B 404     7334   8541   8352     -2   -178   -197       C  
HETATM 5300  C13 OLC B 404     -35.626  34.230  34.502  1.00 47.29           C  
ANISOU 5300  C13 OLC B 404     5282   6500   6187      1   -240   -207       C  
HETATM 5301  C6  OLC B 404     -34.145  34.695  26.510  1.00 61.39           C  
ANISOU 5301  C6  OLC B 404     7003   8680   7644    177   -482   -206       C  
HETATM 5302  C14 OLC B 404     -36.596  35.175  35.168  1.00 59.58           C  
ANISOU 5302  C14 OLC B 404     6814   8054   7770     35   -218   -178       C  
HETATM 5303  C5  OLC B 404     -34.082  33.953  25.202  1.00 56.86           C  
ANISOU 5303  C5  OLC B 404     6402   8187   7014    175   -530   -253       C  
HETATM 5304  C4  OLC B 404     -34.770  34.660  24.055  1.00 68.88           C  
ANISOU 5304  C4  OLC B 404     7878   9816   8477    246   -571   -230       C  
HETATM 5305  C3  OLC B 404     -34.441  36.139  23.956  1.00 69.49           C  
ANISOU 5305  C3  OLC B 404     7991   9880   8532    320   -550   -136       C  
HETATM 5306  C2  OLC B 404     -35.027  36.801  22.740  1.00 73.68           C  
ANISOU 5306  C2  OLC B 404     8481  10518   8996    398   -589   -106       C  
HETATM 5307  C21 OLC B 404     -35.857  38.066  20.606  1.00 62.75           C  
ANISOU 5307  C21 OLC B 404     7037   9322   7485    548   -652    -36       C  
HETATM 5308  C1  OLC B 404     -34.846  38.299  22.752  1.00 80.89           C  
ANISOU 5308  C1  OLC B 404     9425  11410   9901    472   -559     -9       C  
HETATM 5309  C22 OLC B 404     -36.323  38.971  19.488  1.00 62.79           C  
ANISOU 5309  C22 OLC B 404     7013   9428   7418    647   -679     22       C  
HETATM 5310  O19 OLC B 404     -34.354  38.906  23.668  1.00 81.79           O  
ANISOU 5310  O19 OLC B 404     9587  11431  10060    466   -510     33       O  
HETATM 5311  O20 OLC B 404     -35.288  38.895  21.643  1.00 77.75           O  
ANISOU 5311  O20 OLC B 404     8996  11107   9440    548   -590     26       O  
HETATM 5312  C10 OLC B 405      -4.549  38.321  41.339  1.00 65.09           C  
ANISOU 5312  C10 OLC B 405     8292   7984   8454   -189   -101   -138       C  
HETATM 5313  C9  OLC B 405      -4.502  37.037  41.594  1.00 63.10           C  
ANISOU 5313  C9  OLC B 405     8046   7758   8172   -189   -118   -137       C  
HETATM 5314  C11 OLC B 405      -4.507  38.937  39.975  1.00 61.05           C  
ANISOU 5314  C11 OLC B 405     7777   7456   7963   -182    -80   -109       C  
HETATM 5315  C8  OLC B 405      -4.514  36.396  42.948  1.00 55.56           C  
ANISOU 5315  C8  OLC B 405     7096   6820   7193   -190   -135   -159       C  
HETATM 5316  C24 OLC B 405      -7.947  31.852  52.702  1.00 41.87           C  
ANISOU 5316  C24 OLC B 405     5466   5246   5198    -84   -135   -179       C  
HETATM 5317  C7  OLC B 405      -5.665  35.461  43.148  1.00 50.73           C  
ANISOU 5317  C7  OLC B 405     6496   6226   6553   -183   -136   -147       C  
HETATM 5318  C6  OLC B 405      -5.650  34.756  44.498  1.00 53.15           C  
ANISOU 5318  C6  OLC B 405     6810   6550   6833   -179   -148   -161       C  
HETATM 5319  C5  OLC B 405      -6.870  33.916  44.786  1.00 47.48           C  
ANISOU 5319  C5  OLC B 405     6103   5844   6094   -173   -141   -149       C  
HETATM 5320  C4  OLC B 405      -6.909  33.412  46.208  1.00 42.82           C  
ANISOU 5320  C4  OLC B 405     5522   5268   5477   -164   -145   -159       C  
HETATM 5321  C3  OLC B 405      -8.241  32.865  46.650  1.00 41.80           C  
ANISOU 5321  C3  OLC B 405     5403   5146   5334   -158   -131   -149       C  
HETATM 5322  C2  OLC B 405      -8.324  32.718  48.137  1.00 37.97           C  
ANISOU 5322  C2  OLC B 405     4930   4676   4823   -146   -131   -160       C  
HETATM 5323  C21 OLC B 405      -7.179  30.462  50.724  1.00 50.12           C  
ANISOU 5323  C21 OLC B 405     6497   6265   6280   -102   -136   -142       C  
HETATM 5324  C1  OLC B 405      -7.511  31.588  48.692  1.00 44.14           C  
ANISOU 5324  C1  OLC B 405     5719   5472   5580   -136   -137   -151       C  
HETATM 5325  C22 OLC B 405      -7.072  30.722  52.211  1.00 50.48           C  
ANISOU 5325  C22 OLC B 405     6553   6338   6287    -81   -141   -156       C  
HETATM 5326  O19 OLC B 405      -7.051  30.686  48.051  1.00 55.98           O  
ANISOU 5326  O19 OLC B 405     7216   6969   7084   -138   -138   -135       O  
HETATM 5327  O25 OLC B 405      -7.363  33.117  52.419  1.00 53.68           O  
ANISOU 5327  O25 OLC B 405     6948   6736   6714    -98   -153   -213       O  
HETATM 5328  O23 OLC B 405      -7.387  29.529  52.929  1.00 57.11           O  
ANISOU 5328  O23 OLC B 405     7410   7190   7099    -59   -123   -127       O  
HETATM 5329  O20 OLC B 405      -7.332  31.707  50.005  1.00 47.35           O  
ANISOU 5329  O20 OLC B 405     6134   5898   5958   -121   -142   -162       O  
HETATM 5330  C1  PLM B 406     -17.563  53.720  21.346  1.00 67.94           C  
ANISOU 5330  C1  PLM B 406     8600   8581   8632    824    375    972       C  
HETATM 5331  O2  PLM B 406     -17.562  54.987  21.409  1.00 69.94           O  
ANISOU 5331  O2  PLM B 406     8866   8767   8942    863    443   1031       O  
HETATM 5332  C2  PLM B 406     -17.031  52.968  22.615  1.00 68.04           C  
ANISOU 5332  C2  PLM B 406     8616   8548   8689    726    346    876       C  
HETATM 5333  C3  PLM B 406     -16.218  53.828  23.597  1.00 67.15           C  
ANISOU 5333  C3  PLM B 406     8524   8315   8675    684    406    864       C  
HETATM 5334  C4  PLM B 406     -15.672  53.063  24.825  1.00 75.15           C  
ANISOU 5334  C4  PLM B 406     9539   9294   9722    594    374    772       C  
HETATM 5335  C5  PLM B 406     -14.653  53.872  25.650  1.00 68.16           C  
ANISOU 5335  C5  PLM B 406     8673   8297   8929    552    431    756       C  
HETATM 5336  C6  PLM B 406     -14.132  53.169  26.908  1.00 64.37           C  
ANISOU 5336  C6  PLM B 406     8193   7789   8477    469    398    667       C  
HETATM 5337  C10 OLC B 407     -14.660  17.986  46.685  1.00 44.73           C  
ANISOU 5337  C10 OLC B 407     5791   5339   5866   -231    201    -40       C  
HETATM 5338  C9  OLC B 407     -15.153  16.841  46.284  1.00 52.69           C  
ANISOU 5338  C9  OLC B 407     6789   6313   6918   -254    238    -51       C  
HETATM 5339  C11 OLC B 407     -13.782  18.823  45.812  1.00 47.63           C  
ANISOU 5339  C11 OLC B 407     6155   5733   6209   -231    149    -56       C  
HETATM 5340  C8  OLC B 407     -15.779  15.775  47.125  1.00 53.82           C  
ANISOU 5340  C8  OLC B 407     6939   6417   7094   -254    301    -29       C  
HETATM 5341  C12 OLC B 407     -13.312  20.085  46.453  1.00 39.81           C  
ANISOU 5341  C12 OLC B 407     5175   4774   5177   -206    116    -44       C  
HETATM 5342  C7  OLC B 407     -15.011  14.492  47.085  1.00 60.49           C  
ANISOU 5342  C7  OLC B 407     7801   7222   7961   -248    337    -12       C  
HETATM 5343  C13 OLC B 407     -12.312  20.843  45.601  1.00 40.19           C  
ANISOU 5343  C13 OLC B 407     5220   4843   5208   -205     72    -56       C  
HETATM 5344  O   HOH A 501      12.733  14.638  62.145  1.00 54.93           O  
ANISOU 5344  O   HOH A 501     6959   7653   6260    882   -337    474       O  
HETATM 5345  O   HOH A 502       2.138  20.823   8.819  1.00 43.01           O  
ANISOU 5345  O   HOH A 502     5685   5910   4749    125    131   -317       O  
HETATM 5346  O   HOH A 503       4.992  34.575  20.032  1.00 29.50           O  
ANISOU 5346  O   HOH A 503     3840   3626   3741     42    228    252       O  
HETATM 5347  O   HOH A 504      -3.795  20.821  57.878  1.00 64.10           O  
ANISOU 5347  O   HOH A 504     8394   8188   7772    219    -16    165       O  
HETATM 5348  O   HOH A 505       0.023  15.228  12.535  1.00 46.31           O  
ANISOU 5348  O   HOH A 505     6052   6124   5422   -104     82   -614       O  
HETATM 5349  O   HOH A 506      16.596  30.040  10.794  1.00 34.46           O  
ANISOU 5349  O   HOH A 506     4499   4267   4326    198    697    371       O  
HETATM 5350  O   HOH A 507      18.524  21.875   1.902  1.00 42.44           O  
ANISOU 5350  O   HOH A 507     5724   5593   4807    419    906    129       O  
HETATM 5351  O   HOH A 508      13.618  20.287  59.200  1.00 35.96           O  
ANISOU 5351  O   HOH A 508     4407   5215   4042    546   -517     94       O  
HETATM 5352  O   HOH A 509      17.102   3.460  18.617  1.00 33.99           O  
ANISOU 5352  O   HOH A 509     4540   3697   4678     71    733   -331       O  
HETATM 5353  O   HOH A 510       0.562  14.256  26.577  1.00 26.16           O  
ANISOU 5353  O   HOH A 510     3462   3061   3414   -230    109   -311       O  
HETATM 5354  O   HOH A 511      10.253  25.259   0.513  1.00 55.15           O  
ANISOU 5354  O   HOH A 511     7391   7581   5982    526    611    137       O  
HETATM 5355  O   HOH A 512      11.967  25.684  15.323  1.00 25.67           O  
ANISOU 5355  O   HOH A 512     3395   3195   3164     62    370    103       O  
HETATM 5356  O   HOH A 513       4.641  34.418  10.035  1.00 41.20           O  
ANISOU 5356  O   HOH A 513     5452   5459   4741    368    399    446       O  
HETATM 5357  O   HOH A 514       9.556  20.520  56.917  1.00 31.30           O  
ANISOU 5357  O   HOH A 514     3953   4364   3574    390   -367    106       O  
HETATM 5358  O   HOH A 515      -2.620  30.465  19.471  1.00 28.84           O  
ANISOU 5358  O   HOH A 515     3761   3817   3378     45    -12     54       O  
HETATM 5359  O   HOH A 516      -8.399  23.868  60.603  1.00 43.75           O  
ANISOU 5359  O   HOH A 516     5861   5641   5120    200     38     94       O  
HETATM 5360  O   HOH A 517      17.448  32.678  57.788  1.00 42.58           O  
ANISOU 5360  O   HOH A 517     4848   6083   5247     37   -795   -684       O  
HETATM 5361  O   HOH A 518      10.499  23.308  23.486  1.00 24.44           O  
ANISOU 5361  O   HOH A 518     3168   2915   3206    -79    162     -7       O  
HETATM 5362  O   HOH A 519       5.680  19.248  51.289  1.00 32.77           O  
ANISOU 5362  O   HOH A 519     4244   4195   4011    185   -168    131       O  
HETATM 5363  O   HOH A 520      10.766  19.827  40.434  1.00 21.18           O  
ANISOU 5363  O   HOH A 520     2660   2537   2849      2   -101     36       O  
HETATM 5364  O   HOH A 521       2.296  26.259  15.631  1.00 32.49           O  
ANISOU 5364  O   HOH A 521     4284   4296   3764     57    103    -24       O  
HETATM 5365  O   HOH A 522      10.213  22.983  38.842  1.00 26.50           O  
ANISOU 5365  O   HOH A 522     3316   3206   3547    -74   -121    -20       O  
HETATM 5366  O   HOH A 523      18.613  23.477  54.329  1.00 38.03           O  
ANISOU 5366  O   HOH A 523     4406   5398   4645    316   -605   -130       O  
HETATM 5367  O   HOH A 524      17.209  25.066  17.111  1.00 21.76           O  
ANISOU 5367  O   HOH A 524     2793   2563   2911     32    459    137       O  
HETATM 5368  O   HOH A 525       5.459  18.413   4.644  1.00 35.67           O  
ANISOU 5368  O   HOH A 525     4838   5051   3663    209    286   -408       O  
HETATM 5369  O   HOH A 526      17.819  27.783  10.299  1.00 34.63           O  
ANISOU 5369  O   HOH A 526     4525   4300   4334    198    712    309       O  
HETATM 5370  O   HOH A 527      13.505  20.617  20.933  1.00 25.41           O  
ANISOU 5370  O   HOH A 527     3299   3020   3334    -33    276    -20       O  
HETATM 5371  O   HOH A 528      -7.294  30.538  59.742  1.00 40.03           O  
ANISOU 5371  O   HOH A 528     5311   5213   4685     81   -139   -183       O  
HETATM 5372  O   HOH A 529      21.537  17.367  13.531  1.00 44.99           O  
ANISOU 5372  O   HOH A 529     5785   5476   5832    134    668     15       O  
HETATM 5373  O   HOH A 530      -0.732  26.919  19.930  1.00 25.22           O  
ANISOU 5373  O   HOH A 530     3316   3306   2960    -29     -3    -53       O  
HETATM 5374  O   HOH A 531       3.847  30.607  10.052  1.00 30.88           O  
ANISOU 5374  O   HOH A 531     4144   4242   3347    298    281    240       O  
HETATM 5375  O   HOH A 532      12.803  14.328   4.301  1.00 35.77           O  
ANISOU 5375  O   HOH A 532     4902   4765   3924    206    596   -422       O  
HETATM 5376  O   HOH A 533      13.551   7.713  18.615  1.00 26.80           O  
ANISOU 5376  O   HOH A 533     3619   2973   3592    -19    528   -340       O  
HETATM 5377  O   HOH A 534      -3.881  37.858  19.340  1.00 41.80           O  
ANISOU 5377  O   HOH A 534     5401   5392   5088    199    101    334       O  
HETATM 5378  O   HOH A 535      10.047  17.787   1.107  1.00 35.21           O  
ANISOU 5378  O   HOH A 535     4866   5004   3508    338    522   -346       O  
HETATM 5379  O   HOH A 536       8.571  24.292  14.108  1.00 25.15           O  
ANISOU 5379  O   HOH A 536     3378   3249   2929     73    288      7       O  
HETATM 5380  O   HOH A 537      -3.187  41.004  14.196  1.00 51.23           O  
ANISOU 5380  O   HOH A 537     6651   6688   6127    447    276    608       O  
HETATM 5381  O   HOH A 538      12.630   7.504  15.599  1.00 36.45           O  
ANISOU 5381  O   HOH A 538     4880   4268   4702    -33    550   -462       O  
HETATM 5382  O   HOH A 539      20.313  24.102   9.809  1.00 35.95           O  
ANISOU 5382  O   HOH A 539     4682   4448   4530    199    763    215       O  
HETATM 5383  O   HOH A 540      23.246  26.356  15.344  1.00 45.48           O  
ANISOU 5383  O   HOH A 540     5673   5482   6127     67    689    248       O  
HETATM 5384  O   HOH A 541      17.750  25.234  29.626  1.00 22.45           O  
ANISOU 5384  O   HOH A 541     2670   2607   3254    -96    107     26       O  
HETATM 5385  O   HOH A 542       6.185  18.908  28.028  1.00 24.45           O  
ANISOU 5385  O   HOH A 542     3208   2870   3214   -136     73   -106       O  
HETATM 5386  O   HOH A 543      13.539  25.799  41.969  1.00 26.50           O  
ANISOU 5386  O   HOH A 543     3175   3312   3581    -67   -232    -88       O  
HETATM 5387  O   HOH A 544      14.253  25.807  16.997  1.00 23.05           O  
ANISOU 5387  O   HOH A 544     3007   2778   2975     30    392    123       O  
HETATM 5388  O   HOH A 545       6.756  31.106  57.979  1.00 47.08           O  
ANISOU 5388  O   HOH A 545     5884   6364   5642     74   -513   -393       O  
HETATM 5389  O   HOH A 546       7.921  35.856  17.389  1.00 32.55           O  
ANISOU 5389  O   HOH A 546     4234   3975   4160    100    388    365       O  
HETATM 5390  O   HOH A 547      22.074  32.858  14.555  1.00 45.18           O  
ANISOU 5390  O   HOH A 547     5625   5364   6178     53    805    408       O  
HETATM 5391  O   HOH A 548      -9.493  33.104  19.974  1.00 45.90           O  
ANISOU 5391  O   HOH A 548     5838   6149   5452    125   -136     76       O  
HETATM 5392  O   HOH A 549       3.777  40.014  15.664  1.00 46.30           O  
ANISOU 5392  O   HOH A 549     6020   5778   5792    260    433    550       O  
HETATM 5393  O   HOH A 550      13.331  32.500  12.985  1.00 28.17           O  
ANISOU 5393  O   HOH A 550     3698   3458   3546    164    578    386       O  
HETATM 5394  O   HOH A 551      14.600  23.278  54.482  1.00 41.67           O  
ANISOU 5394  O   HOH A 551     5041   5739   5052    283   -513    -77       O  
HETATM 5395  O   HOH A 552      15.014   6.799  16.239  1.00 31.03           O  
ANISOU 5395  O   HOH A 552     4177   3511   4101     15    616   -391       O  
HETATM 5396  O   HOH A 553      18.995  19.582  56.352  1.00 45.90           O  
ANISOU 5396  O   HOH A 553     5454   6499   5489    549   -579     78       O  
HETATM 5397  O   HOH A 554      22.830  34.491  10.498  1.00 42.11           O  
ANISOU 5397  O   HOH A 554     5301   4979   5718    169   1041    578       O  
HETATM 5398  O   HOH A 555       0.666  23.909  18.063  1.00 31.01           O  
ANISOU 5398  O   HOH A 555     4074   4061   3648    -37     32   -144       O  
HETATM 5399  O   HOH A 556       7.188  41.713  15.059  1.00 58.92           O  
ANISOU 5399  O   HOH A 556     7603   7226   7558    250    614    641       O  
HETATM 5400  O   HOH A 557      10.274  29.388   4.304  1.00 48.91           O  
ANISOU 5400  O   HOH A 557     6523   6560   5500    456    613    354       O  
HETATM 5401  O   HOH A 558      19.442  10.648   8.751  1.00 45.61           O  
ANISOU 5401  O   HOH A 558     6055   5594   5680    173    792   -313       O  
HETATM 5402  O   HOH A 559       2.869  13.517  19.143  1.00 34.03           O  
ANISOU 5402  O   HOH A 559     4496   4198   4234   -178    171   -452       O  
HETATM 5403  O   HOH A 560      14.193  27.270   3.176  1.00 35.37           O  
ANISOU 5403  O   HOH A 560     4817   4770   3852    447    764    322       O  
HETATM 5404  O   HOH A 561      20.209  24.247   6.678  1.00 38.35           O  
ANISOU 5404  O   HOH A 561     5057   4841   4673    287    861    247       O  
HETATM 5405  O   HOH A 562      20.384  26.534   7.118  1.00 49.61           O  
ANISOU 5405  O   HOH A 562     6453   6230   6165    284    887    341       O  
HETATM 5406  O   HOH A 563      -0.955  28.921  13.805  1.00 46.94           O  
ANISOU 5406  O   HOH A 563     6106   6293   5434    162     53     47       O  
HETATM 5407  O   HOH A 564       8.350  27.975  55.612  1.00 28.58           O  
ANISOU 5407  O   HOH A 564     3531   3966   3363    111   -472   -238       O  
HETATM 5408  O   HOH A 565      22.377  22.081  14.731  1.00 37.31           O  
ANISOU 5408  O   HOH A 565     4720   4492   4965    102    652    147       O  
HETATM 5409  O   HOH A 566      14.540  39.365  14.903  1.00 32.64           O  
ANISOU 5409  O   HOH A 566     4173   3762   4467    121    760    566       O  
HETATM 5410  O   HOH A 567       2.502  14.560  61.360  1.00 50.98           O  
ANISOU 5410  O   HOH A 567     6752   6705   5913    618     24    500       O  
HETATM 5411  O   HOH A 568       7.375  22.956  38.822  1.00 28.87           O  
ANISOU 5411  O   HOH A 568     3672   3485   3810    -98   -111    -26       O  
HETATM 5412  O   HOH A 569      -1.819  24.575  13.809  1.00 43.96           O  
ANISOU 5412  O   HOH A 569     5717   5948   5037     65    -11   -181       O  
HETATM 5413  O   HOH A 570      11.872  24.775  37.574  1.00 27.96           O  
ANISOU 5413  O   HOH A 570     3450   3388   3787   -100   -117    -38       O  
HETATM 5414  O   HOH A 571      -3.821  17.756  16.048  1.00 37.35           O  
ANISOU 5414  O   HOH A 571     4839   4991   4363   -150    -46   -529       O  
HETATM 5415  O   HOH A 572      19.332  41.102  14.519  1.00 54.56           O  
ANISOU 5415  O   HOH A 572     6830   6353   7546     62    990    623       O  
HETATM 5416  O   HOH A 573      13.667  18.224  19.670  1.00 26.08           O  
ANISOU 5416  O   HOH A 573     3419   3100   3391    -18    320    -74       O  
HETATM 5417  O   HOH A 574      20.490  12.671   8.388  1.00 59.94           O  
ANISOU 5417  O   HOH A 574     7845   7442   7489    202    810   -211       O  
HETATM 5418  O   HOH A 575       5.586  19.287  30.802  1.00 35.84           O  
ANISOU 5418  O   HOH A 575     4640   4300   4679   -140     35    -82       O  
HETATM 5419  O   HOH A 576       2.190  41.864  18.331  1.00 40.78           O  
ANISOU 5419  O   HOH A 576     5293   4988   5214    214    398    531       O  
HETATM 5420  O   HOH A 577      -0.505  35.803  10.150  1.00 48.07           O  
ANISOU 5420  O   HOH A 577     6300   6500   5463    449    250    456       O  
HETATM 5421  O   HOH A 578      15.521   4.288  16.224  1.00 33.72           O  
ANISOU 5421  O   HOH A 578     4539   3753   4519     24    705   -445       O  
HETATM 5422  O   HOH A 579       6.329  25.260   4.027  1.00 46.79           O  
ANISOU 5422  O   HOH A 579     6257   6495   5026    393    376     31       O  
HETATM 5423  O   HOH A 580      21.049   6.221  13.257  1.00 41.67           O  
ANISOU 5423  O   HOH A 580     5501   4832   5498    158    833   -309       O  
HETATM 5424  O   HOH A 581      19.686  16.098   4.529  1.00 64.36           O  
ANISOU 5424  O   HOH A 581     8466   8199   7790    292    857   -128       O  
HETATM 5425  O   HOH A 582      14.083  34.015   2.876  1.00 57.65           O  
ANISOU 5425  O   HOH A 582     7629   7495   6782    564    946    702       O  
HETATM 5426  O   HOH A 583      -0.802  20.562  10.567  1.00 50.98           O  
ANISOU 5426  O   HOH A 583     6640   6929   5800     57     23   -391       O  
HETATM 5427  O   HOH A 584       7.757  38.524  16.660  1.00 41.95           O  
ANISOU 5427  O   HOH A 584     5429   5118   5393    150    478    474       O  
HETATM 5428  O   HOH A 585       2.160  22.180   5.632  1.00 55.41           O  
ANISOU 5428  O   HOH A 585     7288   7659   6104    256    158   -262       O  
HETATM 5429  O   HOH A 586      20.871   8.940   6.245  1.00 59.06           O  
ANISOU 5429  O   HOH A 586     7804   7303   7332    228    925   -390       O  
HETATM 5430  O   HOH A 587      -0.356  26.080  15.618  1.00 54.74           O  
ANISOU 5430  O   HOH A 587     7086   7193   6520     53     30    -78       O  
HETATM 5431  O   HOH A 588       9.565  25.146  -2.454  1.00 56.55           O  
ANISOU 5431  O   HOH A 588     7624   7963   5901    652    632    126       O  
HETATM 5432  O   HOH A 589      -1.858  27.117  17.363  1.00 43.26           O  
ANISOU 5432  O   HOH A 589     5607   5714   5116     31    -13    -60       O  
HETATM 5433  O   HOH A 590      22.152  22.041  10.346  1.00 53.22           O  
ANISOU 5433  O   HOH A 590     6835   6587   6797    189    790    169       O  
HETATM 5434  O   HOH A 591       4.347  23.775   4.138  1.00 51.65           O  
ANISOU 5434  O   HOH A 591     6856   7186   5583    353    274   -111       O  
HETATM 5435  O   HOH B 501      -4.477  25.567  66.108  1.00 56.85           O  
ANISOU 5435  O   HOH B 501     7533   7656   6412    413   -132     17       O  
HETATM 5436  O   HOH B 502     -26.504  11.658  56.037  1.00 46.94           O  
ANISOU 5436  O   HOH B 502     6018   5276   6539   -254    964    192       O  
HETATM 5437  O   HOH B 503     -16.938  36.195  16.100  1.00 40.24           O  
ANISOU 5437  O   HOH B 503     4960   5886   4443    413   -288    171       O  
HETATM 5438  O   HOH B 504     -21.930  49.361  62.187  1.00 44.57           O  
ANISOU 5438  O   HOH B 504     5891   5346   5697     53    311   -611       O  
HETATM 5439  O   HOH B 505     -23.803  25.706  17.403  1.00 49.97           O  
ANISOU 5439  O   HOH B 505     5850   7347   5789    -24   -570   -607       O  
HETATM 5440  O   HOH B 506     -26.520  25.823  65.323  1.00 31.60           O  
ANISOU 5440  O   HOH B 506     4301   3884   3819    143    669    167       O  
HETATM 5441  O   HOH B 507     -23.464  21.412  67.287  1.00 51.80           O  
ANISOU 5441  O   HOH B 507     6980   6449   6254    267    761    358       O  
HETATM 5442  O   HOH B 508     -20.424  33.654  36.512  1.00 27.03           O  
ANISOU 5442  O   HOH B 508     3303   3468   3498   -109   -143    -90       O  
HETATM 5443  O   HOH B 509     -30.006  42.348  48.670  1.00 30.72           O  
ANISOU 5443  O   HOH B 509     3748   3751   4174     69    186    -68       O  
HETATM 5444  O   HOH B 510     -25.050  37.350  24.020  1.00 28.45           O  
ANISOU 5444  O   HOH B 510     3238   4266   3305    279   -353     63       O  
HETATM 5445  O   HOH B 511     -21.205  36.087  18.234  1.00 34.69           O  
ANISOU 5445  O   HOH B 511     4120   5245   3815    377   -383     84       O  
HETATM 5446  O   HOH B 512     -25.658  22.060  65.221  1.00 41.34           O  
ANISOU 5446  O   HOH B 512     5559   5048   5100    150    764    286       O  
HETATM 5447  O   HOH B 513     -20.091  33.279  51.795  1.00 22.13           O  
ANISOU 5447  O   HOH B 513     2899   2664   2845   -102     74   -124       O  
HETATM 5448  O   HOH B 514     -25.561  21.900  55.284  1.00 30.65           O  
ANISOU 5448  O   HOH B 514     3950   3594   4102   -163    483     43       O  
HETATM 5449  O   HOH B 515     -13.112  23.960  17.469  1.00 43.16           O  
ANISOU 5449  O   HOH B 515     5372   6045   4982    -68   -303   -437       O  
HETATM 5450  O   HOH B 516     -13.755  26.672  64.303  1.00 32.41           O  
ANISOU 5450  O   HOH B 516     4485   4237   3592    231    167     48       O  
HETATM 5451  O   HOH B 517     -28.577  35.249  66.310  1.00 42.89           O  
ANISOU 5451  O   HOH B 517     5707   5389   5199    174    558   -114       O  
HETATM 5452  O   HOH B 518     -11.829  34.713  72.985  1.00 42.52           O  
ANISOU 5452  O   HOH B 518     5841   5970   4343    413    -21   -414       O  
HETATM 5453  O   HOH B 519     -20.349  31.123  74.331  1.00 45.24           O  
ANISOU 5453  O   HOH B 519     6300   6109   4780    500    456    -39       O  
HETATM 5454  O   HOH B 520     -12.021  33.157  20.884  1.00 37.83           O  
ANISOU 5454  O   HOH B 520     4768   5172   4435    118   -190     40       O  
HETATM 5455  O   HOH B 521     -12.599  28.944  64.906  1.00 31.57           O  
ANISOU 5455  O   HOH B 521     4368   4199   3427    230     77    -60       O  
HETATM 5456  O   HOH B 522     -19.906  36.729  34.781  1.00 21.00           O  
ANISOU 5456  O   HOH B 522     2545   2718   2715    -23   -141     -9       O  
HETATM 5457  O   HOH B 523     -17.006  30.773  33.401  1.00 27.76           O  
ANISOU 5457  O   HOH B 523     3434   3585   3528   -150   -178   -128       O  
HETATM 5458  O   HOH B 524     -25.169  37.822  70.680  1.00 41.09           O  
ANISOU 5458  O   HOH B 524     5630   5320   4660    287    486   -283       O  
HETATM 5459  O   HOH B 525     -16.292  33.161  20.672  1.00 39.83           O  
ANISOU 5459  O   HOH B 525     4917   5587   4632    152   -286    -15       O  
HETATM 5460  O   HOH B 526     -12.866  31.368  45.551  1.00 22.98           O  
ANISOU 5460  O   HOH B 526     3002   2763   2966   -166    -80   -115       O  
HETATM 5461  O   HOH B 527     -33.328  26.129  55.750  1.00 28.66           O  
ANISOU 5461  O   HOH B 527     3479   3407   4004   -178    565    -32       O  
HETATM 5462  O   HOH B 528     -26.468  16.726  59.582  1.00 39.01           O  
ANISOU 5462  O   HOH B 528     5104   4497   5220    -87    839    253       O  
HETATM 5463  O   HOH B 529     -12.337  18.795  63.778  1.00 40.18           O  
ANISOU 5463  O   HOH B 529     5523   5088   4656    334    374    369       O  
HETATM 5464  O   HOH B 530     -11.230  40.814  70.308  1.00 53.00           O  
ANISOU 5464  O   HOH B 530     7061   7105   5971    186   -102   -749       O  
HETATM 5465  O   HOH B 531     -18.611  31.006  59.801  1.00 22.67           O  
ANISOU 5465  O   HOH B 531     3129   2827   2656     34    177    -88       O  
HETATM 5466  O   HOH B 532     -17.160  36.002  54.370  1.00 26.85           O  
ANISOU 5466  O   HOH B 532     3563   3276   3364    -68     35   -200       O  
HETATM 5467  O   HOH B 533     -10.503  32.691  68.724  1.00 39.39           O  
ANISOU 5467  O   HOH B 533     5373   5410   4182    305    -55   -287       O  
HETATM 5468  O   HOH B 534     -24.525  37.547  47.107  1.00 21.46           O  
ANISOU 5468  O   HOH B 534     2662   2597   2894    -64     58   -100       O  
HETATM 5469  O   HOH B 535     -31.407  29.564  55.268  1.00 24.39           O  
ANISOU 5469  O   HOH B 535     3000   2924   3345   -118    429    -56       O  
HETATM 5470  O   HOH B 536     -10.256  32.451  65.436  1.00 36.10           O  
ANISOU 5470  O   HOH B 536     4904   4858   3954    202    -68   -257       O  
HETATM 5471  O   HOH B 537     -28.380  30.424  59.702  1.00 31.70           O  
ANISOU 5471  O   HOH B 537     4123   3869   4052     -8    463    -21       O  
HETATM 5472  O   HOH B 538     -16.373  30.816  58.306  1.00 20.53           O  
ANISOU 5472  O   HOH B 538     2846   2556   2398      8    100   -102       O  
HETATM 5473  O   HOH B 539     -27.664  43.012  56.174  1.00 31.52           O  
ANISOU 5473  O   HOH B 539     4056   3775   4147     60    299   -211       O  
HETATM 5474  O   HOH B 540     -11.166  45.785  66.078  1.00 46.60           O  
ANISOU 5474  O   HOH B 540     6155   5980   5572    -12    -68   -896       O  
HETATM 5475  O   HOH B 541     -17.881  43.960  68.477  1.00 48.60           O  
ANISOU 5475  O   HOH B 541     6521   6247   5696    134    155   -692       O  
HETATM 5476  O   HOH B 542     -13.491  31.540  58.065  1.00 21.52           O  
ANISOU 5476  O   HOH B 542     2971   2716   2490      8     11   -147       O  
HETATM 5477  O   HOH B 543     -22.668  20.634  57.854  1.00 30.85           O  
ANISOU 5477  O   HOH B 543     4103   3625   3992    -59    519    146       O  
HETATM 5478  O   HOH B 544     -34.303  18.674  56.013  1.00 43.76           O  
ANISOU 5478  O   HOH B 544     5342   5108   6177   -318    846     10       O  
HETATM 5479  O   HOH B 545     -22.086  32.258  61.149  1.00 24.10           O  
ANISOU 5479  O   HOH B 545     3301   2994   2861     53    280    -93       O  
HETATM 5480  O   HOH B 546     -22.433  28.587  19.845  1.00 35.92           O  
ANISOU 5480  O   HOH B 546     4174   5378   4095     33   -478   -370       O  
HETATM 5481  O   HOH B 547     -17.267  24.262  62.320  1.00 27.08           O  
ANISOU 5481  O   HOH B 547     3778   3392   3118    149    329    140       O  
HETATM 5482  O   HOH B 548     -20.507  38.779  74.209  1.00 42.66           O  
ANISOU 5482  O   HOH B 548     5924   5757   4529    381    326   -468       O  
HETATM 5483  O   HOH B 549      -8.234  34.833  60.431  1.00 34.27           O  
ANISOU 5483  O   HOH B 549     4565   4470   3986     31   -159   -347       O  
HETATM 5484  O   HOH B 550      -7.700  22.276  64.560  1.00 36.62           O  
ANISOU 5484  O   HOH B 550     5028   4877   4007    384     84    206       O  
HETATM 5485  O   HOH B 551     -31.577  27.652  61.660  1.00 44.83           O  
ANISOU 5485  O   HOH B 551     5755   5484   5796     -5    680     65       O  
HETATM 5486  O   HOH B 552      -3.218  29.422  17.041  1.00 51.93           O  
ANISOU 5486  O   HOH B 552     6694   6860   6178     88    -25     18       O  
HETATM 5487  O   HOH B 553     -30.942  20.598  64.980  1.00 44.22           O  
ANISOU 5487  O   HOH B 553     5796   5272   5734     54   1011    312       O  
HETATM 5488  O   HOH B 554     -23.335  33.676  36.528  1.00 27.42           O  
ANISOU 5488  O   HOH B 554     3275   3576   3566    -97   -149   -106       O  
HETATM 5489  O   HOH B 555     -17.920  42.334  71.050  1.00 43.84           O  
ANISOU 5489  O   HOH B 555     5975   5781   4899    220    167   -671       O  
HETATM 5490  O   HOH B 556     -16.258  17.243  60.288  1.00 33.54           O  
ANISOU 5490  O   HOH B 556     4606   4011   4127    137    514    332       O  
HETATM 5491  O   HOH B 557     -34.408  38.726  59.106  1.00 38.92           O  
ANISOU 5491  O   HOH B 557     4882   4778   5129     82    518   -114       O  
HETATM 5492  O   HOH B 558     -18.739  31.813  37.676  1.00 25.11           O  
ANISOU 5492  O   HOH B 558     3105   3172   3263   -160   -129   -116       O  
HETATM 5493  O   HOH B 559     -10.197  30.382  67.856  1.00 49.81           O  
ANISOU 5493  O   HOH B 559     6697   6699   5529    323    -27   -164       O  
HETATM 5494  O   HOH B 560     -30.007  32.619  57.265  1.00 34.86           O  
ANISOU 5494  O   HOH B 560     4424   4269   4551    -38    406    -68       O  
HETATM 5495  O   HOH B 561     -32.277  31.794  61.440  1.00 47.09           O  
ANISOU 5495  O   HOH B 561     6020   5813   6057     29    603    -16       O  
HETATM 5496  O   HOH B 562     -31.382  35.854  64.456  1.00 47.80           O  
ANISOU 5496  O   HOH B 562     6223   5950   5987    133    601    -99       O  
HETATM 5497  O   HOH B 563     -20.260  27.073  71.116  1.00 46.52           O  
ANISOU 5497  O   HOH B 563     6409   6101   5165    421    511    154       O  
HETATM 5498  O   HOH B 564     -16.609  29.203  72.252  1.00 33.85           O  
ANISOU 5498  O   HOH B 564     4818   4676   3368    471    305      3       O  
HETATM 5499  O   HOH B 565     -28.281  14.578  56.975  1.00 40.96           O  
ANISOU 5499  O   HOH B 565     5229   4630   5705   -233    901    167       O  
HETATM 5500  O   HOH B 566     -25.096  37.321  44.540  1.00 33.75           O  
ANISOU 5500  O   HOH B 566     4162   4198   4461    -60     17    -81       O  
HETATM 5501  O   HOH B 567     -16.912  38.265  55.603  1.00 29.14           O  
ANISOU 5501  O   HOH B 567     3867   3559   3646    -54     38   -263       O  
HETATM 5502  O   HOH B 568     -28.609  42.136  13.520  1.00 55.79           O  
ANISOU 5502  O   HOH B 568     6525   8527   6146    961   -519    431       O  
HETATM 5503  O   HOH B 569     -11.702  37.604  19.394  1.00 45.92           O  
ANISOU 5503  O   HOH B 569     5820   6192   5436    284   -100    265       O  
HETATM 5504  O   HOH B 570     -18.944  28.984  73.002  1.00 50.85           O  
ANISOU 5504  O   HOH B 570     6993   6787   5539    486    427     53       O  
HETATM 5505  O   HOH B 571     -31.007  30.316  59.667  1.00 46.71           O  
ANISOU 5505  O   HOH B 571     5957   5753   6039    -22    539    -12       O  
HETATM 5506  O   HOH B 572     -21.329  31.321  77.358  1.00 62.33           O  
ANISOU 5506  O   HOH B 572     8542   8384   6758    622    549    -25       O  
HETATM 5507  O   HOH B 573     -32.701  29.533  57.725  1.00 44.82           O  
ANISOU 5507  O   HOH B 573     5612   5499   5920    -80    540    -24       O  
HETATM 5508  O   HOH B 574     -12.562  42.847  71.586  1.00 60.20           O  
ANISOU 5508  O   HOH B 574     7998   8003   6874    188    -51   -861       O  
HETATM 5509  O   HOH B 575     -34.063  27.081  58.133  1.00 45.99           O  
ANISOU 5509  O   HOH B 575     5720   5605   6151   -118    646      6       O  
HETATM 5510  O   HOH B 576      -7.528  36.580  62.089  1.00 50.73           O  
ANISOU 5510  O   HOH B 576     6646   6610   6020     39   -194   -457       O  
HETATM 5511  O   HOH B 577      -8.694  34.814  65.116  1.00 39.68           O  
ANISOU 5511  O   HOH B 577     5314   5325   4438    151   -152   -396       O  
CONECT    1 5029                                                                
CONECT   13 5052                                                                
CONECT  114 4973                                                                
CONECT  921 1472                                                                
CONECT 1472  921                                                                
CONECT 2270 5046                                                                
CONECT 2485 5156                                                                
CONECT 2487 5256                                                                
CONECT 2499 5279                                                                
CONECT 2600 5001                                                                
CONECT 3404 3965                                                                
CONECT 3965 3404                                                                
CONECT 4755 5273                                                                
CONECT 4971 5330                                                                
CONECT 4973  114 4974 4984                                                      
CONECT 4974 4973 4975 4981                                                      
CONECT 4975 4974 4976 4982                                                      
CONECT 4976 4975 4977 4983                                                      
CONECT 4977 4976 4978 4984                                                      
CONECT 4978 4977 4985                                                           
CONECT 4979 4980 4981 4986                                                      
CONECT 4980 4979                                                                
CONECT 4981 4974 4979                                                           
CONECT 4982 4975                                                                
CONECT 4983 4976 4987                                                           
CONECT 4984 4973 4977                                                           
CONECT 4985 4978                                                                
CONECT 4986 4979                                                                
CONECT 4987 4983 4988 4998                                                      
CONECT 4988 4987 4989 4995                                                      
CONECT 4989 4988 4990 4996                                                      
CONECT 4990 4989 4991 4997                                                      
CONECT 4991 4990 4992 4998                                                      
CONECT 4992 4991 4999                                                           
CONECT 4993 4994 4995 5000                                                      
CONECT 4994 4993                                                                
CONECT 4995 4988 4993                                                           
CONECT 4996 4989                                                                
CONECT 4997 4990                                                                
CONECT 4998 4987 4991                                                           
CONECT 4999 4992                                                                
CONECT 5000 4993                                                                
CONECT 5001 2600 5002 5012                                                      
CONECT 5002 5001 5003 5009                                                      
CONECT 5003 5002 5004 5010                                                      
CONECT 5004 5003 5005 5011                                                      
CONECT 5005 5004 5006 5012                                                      
CONECT 5006 5005 5013                                                           
CONECT 5007 5008 5009 5014                                                      
CONECT 5008 5007                                                                
CONECT 5009 5002 5007                                                           
CONECT 5010 5003                                                                
CONECT 5011 5004 5015                                                           
CONECT 5012 5001 5005                                                           
CONECT 5013 5006                                                                
CONECT 5014 5007                                                                
CONECT 5015 5011 5016 5026                                                      
CONECT 5016 5015 5017 5023                                                      
CONECT 5017 5016 5018 5024                                                      
CONECT 5018 5017 5019 5025                                                      
CONECT 5019 5018 5020 5026                                                      
CONECT 5020 5019 5027                                                           
CONECT 5021 5022 5023 5028                                                      
CONECT 5022 5021                                                                
CONECT 5023 5016 5021                                                           
CONECT 5024 5017                                                                
CONECT 5025 5018                                                                
CONECT 5026 5015 5019                                                           
CONECT 5027 5020                                                                
CONECT 5028 5021                                                                
CONECT 5029    1 5030 5031                                                      
CONECT 5030 5029                                                                
CONECT 5031 5029                                                                
CONECT 5032 5033 5037 5047 5048                                                 
CONECT 5033 5032 5034                                                           
CONECT 5034 5033 5035                                                           
CONECT 5035 5034 5036                                                           
CONECT 5036 5035 5037 5049                                                      
CONECT 5037 5032 5036 5038                                                      
CONECT 5038 5037 5039                                                           
CONECT 5039 5038 5040                                                           
CONECT 5040 5039 5041 5050                                                      
CONECT 5041 5040 5042                                                           
CONECT 5042 5041 5043                                                           
CONECT 5043 5042 5044                                                           
CONECT 5044 5043 5045 5051                                                      
CONECT 5045 5044 5046                                                           
CONECT 5046 2270 5045                                                           
CONECT 5047 5032                                                                
CONECT 5048 5032                                                                
CONECT 5049 5036                                                                
CONECT 5050 5040                                                                
CONECT 5051 5044                                                                
CONECT 5052   13 5053 5063                                                      
CONECT 5053 5052 5054 5060                                                      
CONECT 5054 5053 5055 5061                                                      
CONECT 5055 5054 5056 5062                                                      
CONECT 5056 5055 5057 5063                                                      
CONECT 5057 5056 5064                                                           
CONECT 5058 5059 5060 5065                                                      
CONECT 5059 5058                                                                
CONECT 5060 5053 5058                                                           
CONECT 5061 5054                                                                
CONECT 5062 5055                                                                
CONECT 5063 5052 5056                                                           
CONECT 5064 5057                                                                
CONECT 5065 5058                                                                
CONECT 5066 5068                                                                
CONECT 5067 5068                                                                
CONECT 5068 5066 5067 5069                                                      
CONECT 5069 5068 5070                                                           
CONECT 5070 5069 5071                                                           
CONECT 5071 5070 5072                                                           
CONECT 5072 5071 5073                                                           
CONECT 5073 5072 5074                                                           
CONECT 5074 5073 5075                                                           
CONECT 5075 5074 5076                                                           
CONECT 5076 5075 5077                                                           
CONECT 5077 5076 5078                                                           
CONECT 5078 5077 5079                                                           
CONECT 5079 5078                                                                
CONECT 5080 5083                                                                
CONECT 5081 5082 5084                                                           
CONECT 5082 5081 5085                                                           
CONECT 5083 5080 5087                                                           
CONECT 5084 5081 5088                                                           
CONECT 5085 5082 5089                                                           
CONECT 5086 5100 5102                                                           
CONECT 5087 5083 5090                                                           
CONECT 5088 5084 5091                                                           
CONECT 5089 5085 5092                                                           
CONECT 5090 5087 5093                                                           
CONECT 5091 5088 5093                                                           
CONECT 5092 5089 5094                                                           
CONECT 5093 5090 5091                                                           
CONECT 5094 5092 5095                                                           
CONECT 5095 5094 5096                                                           
CONECT 5096 5095 5097                                                           
CONECT 5097 5096 5099                                                           
CONECT 5098 5100 5104                                                           
CONECT 5099 5097 5101 5104                                                      
CONECT 5100 5086 5098 5103                                                      
CONECT 5101 5099                                                                
CONECT 5102 5086                                                                
CONECT 5103 5100                                                                
CONECT 5104 5098 5099                                                           
CONECT 5105 5106 5107                                                           
CONECT 5106 5105 5108                                                           
CONECT 5107 5105 5110                                                           
CONECT 5108 5106 5111                                                           
CONECT 5109 5122 5124                                                           
CONECT 5110 5107 5113                                                           
CONECT 5111 5108 5114                                                           
CONECT 5112 5115                                                                
CONECT 5113 5110 5115                                                           
CONECT 5114 5111 5116                                                           
CONECT 5115 5112 5113                                                           
CONECT 5116 5114 5117                                                           
CONECT 5117 5116 5118                                                           
CONECT 5118 5117 5119                                                           
CONECT 5119 5118 5121                                                           
CONECT 5120 5122 5126                                                           
CONECT 5121 5119 5123 5126                                                      
CONECT 5122 5109 5120 5125                                                      
CONECT 5123 5121                                                                
CONECT 5124 5109                                                                
CONECT 5125 5122                                                                
CONECT 5126 5120 5121                                                           
CONECT 5127 5128 5129                                                           
CONECT 5128 5127 5130                                                           
CONECT 5129 5127 5131                                                           
CONECT 5130 5128 5132                                                           
CONECT 5131 5129 5133                                                           
CONECT 5132 5130                                                                
CONECT 5133 5131                                                                
CONECT 5134 5135 5136                                                           
CONECT 5135 5134 5137                                                           
CONECT 5136 5134 5138                                                           
CONECT 5137 5135 5139                                                           
CONECT 5138 5136 5140                                                           
CONECT 5139 5137 5141                                                           
CONECT 5140 5138 5142                                                           
CONECT 5141 5139 5143                                                           
CONECT 5142 5140                                                                
CONECT 5143 5141                                                                
CONECT 5144 5145 5146                                                           
CONECT 5145 5144 5147                                                           
CONECT 5146 5144 5148                                                           
CONECT 5147 5145 5149                                                           
CONECT 5148 5146 5150                                                           
CONECT 5149 5147 5151                                                           
CONECT 5150 5148                                                                
CONECT 5151 5149 5152                                                           
CONECT 5152 5151 5153                                                           
CONECT 5153 5152 5154                                                           
CONECT 5154 5153 5155                                                           
CONECT 5155 5154                                                                
CONECT 5156 2485 5157 5158                                                      
CONECT 5157 5156                                                                
CONECT 5158 5156 5159                                                           
CONECT 5159 5158 5160                                                           
CONECT 5160 5159 5161                                                           
CONECT 5161 5160 5162                                                           
CONECT 5162 5161 5163                                                           
CONECT 5163 5162 5164                                                           
CONECT 5164 5163 5165                                                           
CONECT 5165 5164 5166                                                           
CONECT 5166 5165 5167                                                           
CONECT 5167 5166 5168                                                           
CONECT 5168 5167 5169                                                           
CONECT 5169 5168 5170                                                           
CONECT 5170 5169 5171                                                           
CONECT 5171 5170 5172                                                           
CONECT 5172 5171                                                                
CONECT 5173 5174                                                                
CONECT 5174 5173 5175                                                           
CONECT 5175 5174 5176                                                           
CONECT 5176 5175 5177                                                           
CONECT 5177 5176 5178                                                           
CONECT 5178 5177 5179                                                           
CONECT 5179 5178 5180                                                           
CONECT 5180 5179 5181 5182                                                      
CONECT 5181 5180                                                                
CONECT 5182 5180                                                                
CONECT 5183 5186                                                                
CONECT 5184 5185 5187                                                           
CONECT 5185 5184 5188                                                           
CONECT 5186 5183 5190                                                           
CONECT 5187 5184 5191                                                           
CONECT 5188 5185 5192                                                           
CONECT 5189 5203 5205                                                           
CONECT 5190 5186 5193                                                           
CONECT 5191 5187 5194                                                           
CONECT 5192 5188 5195                                                           
CONECT 5193 5190 5196                                                           
CONECT 5194 5191 5196                                                           
CONECT 5195 5192 5197                                                           
CONECT 5196 5193 5194                                                           
CONECT 5197 5195 5198                                                           
CONECT 5198 5197 5199                                                           
CONECT 5199 5198 5200                                                           
CONECT 5200 5199 5202                                                           
CONECT 5201 5203 5207                                                           
CONECT 5202 5200 5204 5207                                                      
CONECT 5203 5189 5201 5206                                                      
CONECT 5204 5202                                                                
CONECT 5205 5189                                                                
CONECT 5206 5203                                                                
CONECT 5207 5201 5202                                                           
CONECT 5208 5209                                                                
CONECT 5209 5208 5210                                                           
CONECT 5210 5209 5211                                                           
CONECT 5211 5210 5212                                                           
CONECT 5212 5211 5213                                                           
CONECT 5213 5212 5214                                                           
CONECT 5214 5213 5215                                                           
CONECT 5215 5214 5216 5217                                                      
CONECT 5216 5215                                                                
CONECT 5217 5215                                                                
CONECT 5218 5221                                                                
CONECT 5219 5220 5222                                                           
CONECT 5220 5219 5223                                                           
CONECT 5221 5218 5225                                                           
CONECT 5222 5219 5226                                                           
CONECT 5223 5220 5227                                                           
CONECT 5224 5238 5240                                                           
CONECT 5225 5221 5228                                                           
CONECT 5226 5222 5229                                                           
CONECT 5227 5223 5230                                                           
CONECT 5228 5225 5231                                                           
CONECT 5229 5226 5231                                                           
CONECT 5230 5227 5232                                                           
CONECT 5231 5228 5229                                                           
CONECT 5232 5230 5233                                                           
CONECT 5233 5232 5234                                                           
CONECT 5234 5233 5235                                                           
CONECT 5235 5234 5237                                                           
CONECT 5236 5238 5242                                                           
CONECT 5237 5235 5239 5242                                                      
CONECT 5238 5224 5236 5241                                                      
CONECT 5239 5237                                                                
CONECT 5240 5224                                                                
CONECT 5241 5238                                                                
CONECT 5242 5236 5237                                                           
CONECT 5243 5244 5245                                                           
CONECT 5244 5243 5246                                                           
CONECT 5245 5243 5247                                                           
CONECT 5246 5244 5248                                                           
CONECT 5247 5245 5249                                                           
CONECT 5248 5246 5250                                                           
CONECT 5249 5247 5251                                                           
CONECT 5250 5248 5252                                                           
CONECT 5251 5249                                                                
CONECT 5252 5250 5253                                                           
CONECT 5253 5252 5254                                                           
CONECT 5254 5253 5255                                                           
CONECT 5255 5254                                                                
CONECT 5256 2487 5257 5258                                                      
CONECT 5257 5256                                                                
CONECT 5258 5256                                                                
CONECT 5259 5260 5264 5274 5275                                                 
CONECT 5260 5259 5261                                                           
CONECT 5261 5260 5262                                                           
CONECT 5262 5261 5263                                                           
CONECT 5263 5262 5264 5276                                                      
CONECT 5264 5259 5263 5265                                                      
CONECT 5265 5264 5266                                                           
CONECT 5266 5265 5267                                                           
CONECT 5267 5266 5268 5277                                                      
CONECT 5268 5267 5269                                                           
CONECT 5269 5268 5270                                                           
CONECT 5270 5269 5271                                                           
CONECT 5271 5270 5272 5278                                                      
CONECT 5272 5271 5273                                                           
CONECT 5273 4755 5272                                                           
CONECT 5274 5259                                                                
CONECT 5275 5259                                                                
CONECT 5276 5263                                                                
CONECT 5277 5267                                                                
CONECT 5278 5271                                                                
CONECT 5279 2499 5280 5290                                                      
CONECT 5280 5279 5281 5287                                                      
CONECT 5281 5280 5282 5288                                                      
CONECT 5282 5281 5283 5289                                                      
CONECT 5283 5282 5284 5290                                                      
CONECT 5284 5283 5291                                                           
CONECT 5285 5286 5287 5292                                                      
CONECT 5286 5285                                                                
CONECT 5287 5280 5285                                                           
CONECT 5288 5281                                                                
CONECT 5289 5282                                                                
CONECT 5290 5279 5283                                                           
CONECT 5291 5284                                                                
CONECT 5292 5285                                                                
CONECT 5293 5294 5295                                                           
CONECT 5294 5293 5296                                                           
CONECT 5295 5293 5297                                                           
CONECT 5296 5294 5298                                                           
CONECT 5297 5295 5300                                                           
CONECT 5298 5296 5301                                                           
CONECT 5299 5302                                                                
CONECT 5300 5297 5302                                                           
CONECT 5301 5298 5303                                                           
CONECT 5302 5299 5300                                                           
CONECT 5303 5301 5304                                                           
CONECT 5304 5303 5305                                                           
CONECT 5305 5304 5306                                                           
CONECT 5306 5305 5308                                                           
CONECT 5307 5309 5311                                                           
CONECT 5308 5306 5310 5311                                                      
CONECT 5309 5307                                                                
CONECT 5310 5308                                                                
CONECT 5311 5307 5308                                                           
CONECT 5312 5313 5314                                                           
CONECT 5313 5312 5315                                                           
CONECT 5314 5312                                                                
CONECT 5315 5313 5317                                                           
CONECT 5316 5325 5327                                                           
CONECT 5317 5315 5318                                                           
CONECT 5318 5317 5319                                                           
CONECT 5319 5318 5320                                                           
CONECT 5320 5319 5321                                                           
CONECT 5321 5320 5322                                                           
CONECT 5322 5321 5324                                                           
CONECT 5323 5325 5329                                                           
CONECT 5324 5322 5326 5329                                                      
CONECT 5325 5316 5323 5328                                                      
CONECT 5326 5324                                                                
CONECT 5327 5316                                                                
CONECT 5328 5325                                                                
CONECT 5329 5323 5324                                                           
CONECT 5330 4971 5331 5332                                                      
CONECT 5331 5330                                                                
CONECT 5332 5330 5333                                                           
CONECT 5333 5332 5334                                                           
CONECT 5334 5333 5335                                                           
CONECT 5335 5334 5336                                                           
CONECT 5336 5335                                                                
CONECT 5337 5338 5339                                                           
CONECT 5338 5337 5340                                                           
CONECT 5339 5337 5341                                                           
CONECT 5340 5338 5342                                                           
CONECT 5341 5339 5343                                                           
CONECT 5342 5340                                                                
CONECT 5343 5341                                                                
MASTER      402    0   26   28    8    0    0    6 5344    2  385   54          
END